Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
The amendment filed March 19, 2026 in response to the Office Action of December 18, 2025 is acknowledged and has been entered.
After an interview on May 7, 2026 requested by applicant, Applicant filed a Supplemental Amendment on May 14, 2026. The amendment is acknowledged. The claims of May 14, 2026 are under examination for this Office Action.
Claims 1, 2, 6, 8, 10, 12, 16, 23, 26, and 27 have been amended.
Claims 14 and 15 have been cancelled.
Claims 34-36 have been added.
Claims 1-13, 16-23, 25-30, and 34-36 are pending and under consideration.
In view of amendment of May 14, 2026, the objection to the drawings set forth in the office action of December 18, 2025 is hereby withdrawn.
In view of amendment of May 14, 2026, the claim objection, 112(b) and 112(d) rejections set forth in the office action of December 18, 2025 are hereby withdrawn.
However, the 103 rejections and Double Patenting rejections are maintained/modified, as shown below.
Information Disclosure Statement
The Information Disclosure Statements filed on 03/19/2026, 06/15/2026 and 06/16/2026 have been considered and entered by examiner.
New Claim Objections
Claim 12 is objected to because of the following informalities: “from 0.006% to 0.01% w/v polysorbate 80” are recited twice. Thus, one of them should be removed. Appropriate correction is required.
Claim 26 is objected to because of the following informalities at 26 (e): “0.01%% w/v polysorbate 80” should be “0.01% w/v polysorbate 80”. Appropriate correction is required.
Claim 27 is objected to because of the following informalities at 27 (e): “0.01%% w/v polysorbate 80” should be “0.01% w/v polysorbate 80”. Appropriate correction is required.
MAINTAINED/MODIFIED REJECTIONS
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-13, 16-23, 25-30, and 34-36 are rejected under 35 U.S.C. 103 as being unpatentable over White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and in view of Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that the specification does not give a specific guidelines attached to the word “about”. A common ±5% range is given to the word “about”. For example, “about 100 mM” means anywhere from 95 mM to 105 mM.
Regarding claim 1, White teaches PVRIG antibody can be used to treat cancers (see [00330]), in particular CHA.7.518.1.H4(S241P) (see [00331-0332]). As evidenced by Fig. 3 of the instant application, CHA.7.518.1.H4(S241P) comprises full length heavy chain of SEQ ID NO: 8 and full length light chain of SEQ ID NO: 13.
White teaches PVRIG antibody (CHA.7.518.1.H4(S241P)) novel cancer immunotherapy agent either as monotherapy or in combination with either TIGIT or PD1 blockade (Example 18).
White teaches as set forth above. However, White does not teach the formulation according to claim 1.
Mhalasakant teaches high concentration stable liquid formulation with optimal osmolality and low viscosity across different temperature excursions and devoid of aggregation.
Mhalasakant teaches a pharmaceutical formulation comprising : a) 1-100 mg/ml of at least one antigen binding protein (overlapping with the range up to 40mg/ml); b) 20-40 mM of Histidine (overlapping with range of instant claim 1(b)); c) 50-100 mM Arginine (overlapping with range of instant claim 1(d)); d) 0.002-0.02% Polysorbate 80 (w/v) (overlapping with range of instant claim 1(e)); e) 50-150 mM NaCl (overlapping with range of instant claim 1(c)); f) not more than 2.5% Sucrose w/v; wherein pH of the formulation is 6.5±0.5 (overlapping with the range 6.5±0.2), wherein the osmolality of the formulation is 300-450 mOsmol/kg and viscosity less than 2.5 mPa-S and said formulation is stable at 2-8 ̊C for at least 9 months, at 25 ̊C for at least 1 months, at 40 ̊C for at least 40 days, at 50 ̊C for at least 2 days (claim 69), wherein the antigen binding protein is an antibody (claim 73).
Mhalasakant teaches that L-Arginine (75 mM) (as the Arginine) is used in the pharmaceutical formulation (Tables 12-18).
Mhalasakant teaches that antibodies are stable in the pharmaceutical formulation at various temperature conditions (Examples 4, 5, 6).
The formulation ranges for each component in the formulation of Mhalasakant are overlapping with the ranges recited by instant claim 1. It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody CHA.7.518.1.H4(S241P) as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of antibody: CHA.7.518.1.H4(S241P).
Regarding claim 2, as shown below, SEQ ID NO: 8 comprises SEQ ID NO: 50:
US-17-631-847-50
Query Match 73.4%; Score 1749; DB 1; Length 327;
Best Local Similarity 100.0%;
Matches 327; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 121 ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS 60
Qy 181 GLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPPCPAPEFLGGPSV 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPPCPAPEFLGGPSV 120
Qy 241 FLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTY 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 FLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTY 180
Qy 301 RVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTK 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTK 240
Qy 361 NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEG 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEG 300
Qy 421 NVFSCSVMHEALHNHYTQKSLSLSPGK 447
|||||||||||||||||||||||||||
Db 301 NVFSCSVMHEALHNHYTQKSLSLSPGK 327
Regarding claim 3, as evidenced by Fig. 4 of the instant application, SEQ ID NO: 50 is from IgG4.
Regarding claim 4, CHA.7.518.1.H4(S241P) comprises full length heavy chain (which includes heavy chain variable domain) of SEQ ID NO: 8 and full length light chain of SEQ ID NO: 13 (which includes light chain variable domain), as evidenced by Fig. 3 of the instant specification.
Regarding claim 5, as shown below, light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO: 13) comprise a CL region of human kappa light chain (IGKC_human):
Query Match 49.4%; Score 553; DB 1; Length 107;
Best Local Similarity 100.0%;
Matches 107; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 108 RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD 167
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD 60
Qy 168 SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 214
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC 107
Regrading claims 6 and 7, the range of 20-40 mM of Histidine taught by Mhalasakant (claim 69) overlaps with the range 20 mM to 25 mM or 25 mM to 30 mM histidine of instant claim 6, and the range about 25 mM histidine of instant claim 7.
Regrading claims 8 and 9, the range of 50-150 mM of NaCl taught by Mhalasakant (claim 69) overlaps with the range 55 mM to 60 mM or 60 mM to 65 mM NaCl of instant claim 8, and the range about 60 mM NaCl of instant claim 9.
Regrading claims 10 and 11, the range of 50-100 mM Arginine (such as 75 mM L-arginine) taught by Mhalasakant (claim 69 and Examples 4-6) overlaps with the range 90 mM to 105 mM or 94 mM to 110 mM L-arginine of instant claim 10, and the range about 100 mM L-arginine of instant claim 11.
Regrading claims 12 and 13, the range of 0.002-0.02% Polysorbate 80 (w/v) taught by Mhalasakant (claim 69) overlaps with the range 0.006% to 0.015% w/v polysorbate 80 of instant claim 12, and the range about 0.01% w/v polysorbate 80 of instant claim 13.
Regarding claim 16, Mhalasakant teaches the range of 6.5±0.5 of pH (claim 69). It would have prima facie been obvious to one of ordinarily skilled in the art before the effective filing date of the claimed invention to make a liquid pharmaceutical formulation with a pH 6.5 which is the central pH value suggested by Mhalasakant.
Regarding claims 17 and 21, the range of 1-100 mg/ml taught by Mhalasakant (claim 69) and 10 mg/mL, or 25mg/mL or 50 mg/mL antibody concentration (Example 3) overlaps with the range 10 mg/mL to 40 mg/mL of instant claim 17, and the range about 20 mg/mL of claim 21.
Regarding claims 18-20, 34 and 35, Mhalasakant teaches that the formulation is stable at 2-8 ̊C for at least 9 months, at 25 ̊C for at least 1 months, at 40 ̊C for at least 40 days, at 50 ̊C for at least 2 days (claim 69 and Examples 4-6).
Regarding claims 22 and 23, as set forth above, antibody CHA.7.518.1.H4 (S241P) reads on the instant claims 2-5. Taken together, CHA.7.518.1.H4 (S241P) reads on claims 22 and 23 which combine the limitations of the instant claims 2-5.
Regarding claim 25, as set forth above, as evidenced by Fig. 3 of the instant application, CHA.7.518.1.H4(S241P) comprises full length heavy chain of SEQ ID NO: 8 and full length light chain of SEQ ID NO: 13.
Regarding claims 26, 27 and 36, as set forth above, White teaches PVRIG antibody (CHA.7.518.1.H4(S241P)) and Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims 26 and 27.
It is also noted that optimum suitable ranges may be obtained by routine experimentation, absent a showing of criticality or unexpected results. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05(II)(A).
Regarding claims 28-30, it is noted that the recitation of “wherein said anti-PVRIG antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti-PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti-PVRIG antibody” (claim 28); “wherein said anti-PVRIG antibody is administered at a dosage of about 0.01 mg/kg, 0.03 mg/kg, 0.1 mg/kg, 0.3 mg/kg, 1 mg/kg, 3 mg/kg, 10 mg/kg, or 20 mg/kg of the anti-PVRIG antibody” (claim 29); or “wherein said anti-PVRIG antibody is administered 20 mg/kg every 4 weeks” (claim 30) is an intended use that does not result in structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art and thus is not given weight for comparison of the claims with the prior art.
Response to Arguments
For the 103 rejection of claims 1-13, 16-23, 25-30, and 34-36 applicant argues:
White does not specify or suggest a stable liquid pharmaceutical formulation of anti-PVRIG antibody with this amino acid composition. Nor does White specify a formulation at pH 6.5 +/- 0.2. Applicant has further amended claim 1 to now recite "wherein the anti-PVRIG antibody is at a concentration of up to 40 mg/mL", a feature which is neither taught nor suggested by the disclosure of White. Thus, White does not teach or suggest all the limitations of currently amended claim 1, nor claim 36….
First and foremost, Mhalasakant also does not teach or suggest a stable liquid pharmaceutical formulation of an anti-PVRIG as presently claimed. Moreover, Applicant respectfully submits that none of these or any other disclosures in Mhalasakant are of particular
relevance to the specific stable liquid pharmaceutical formulation of an anti-PVRIG antibody as
presently claimed.
Applicant’s arguments have been carefully considered, but have not been found persuasive. First, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Although White does not teach the specific formulation for antibody CHA.7.518.1.H4(S241P), as set forth above, Mhalasakant teaches an antibody formulation which comprises the same components in overlapping ranges. Mhalasakant further teaches the formulation have good properties for antibody storage and usage thereby suggesting stability. Therefore, contrary to Applicant’s argument, there are no claim elements missing from the combined teachings of the art above.
Applicant further argues that Mhalasakant’s teaching is limited to Dengue virus antibody and Mhalasakant is non-analogous art, as shown below:
The cited disclosure describes a monoclonal antibody specific to the Dengue virus epitope in domain III of the E protein and IgG 1 monoclonal antibody specific to the rabies virus surface G glycoprotein. Not only does this disclosure indicate that formulation development is a "rate-limiting" (i.e., challenging and difficult) step, the disclosures in Mhalasakant are generic and lack any further details regarding how these excipients are to be specifically applied and/or formulated to achieve a liquid formulation that surprisingly provides for a stable liquid anti-PVRIG antibody pharmaceutical formulation as presently claimed.
Furthermore, Mhalasakant is arguably non-analogous art. The skilled person in the field of cancer treatment looking to develop a stable liquid anti-PVRIG antibody pharmaceutical formulation would not have consulted Mhalasakant because Mhalasakant relates to Dengue monoclonal antibodies and is thus directed to infectious diseases, a completely different disease category, as compared to cancer therapeutics, such as anti-PVRIG antibodies and associated formulations.
Applicant’s arguments have been carefully considered, but have not been found persuasive. Contrary to Applicant’s arguments, Mhalasakant’s teachings are not limited to the Dengue virus antibody. As discussed above, claim 69 recites “one antigen binding protein” (not limited to the specific antibody as Applicant argued), which would including a broad genus of antibodies (as evidenced by claim 73). In addition, Mhalasakant clear teaches that the invention encompasses a broad genus of antibodies, including antibodies to different antigens and antibodies for cancer therapy such as (see the bottom the bridging paragraph of pages 6-7). Thus, the teachings is not limited to infectious diseases. Combining the teachings of White and Mhalasakant, one of ordinary skill in the art would have recognized that the formulation taught by Mhalasakant could be applied to antibody taught by White, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of antibody: CHA.7.518.1.H4(S241P).
Applicant further argues that Examiner employs improper hindsight, as shown below:
Additionally, Applicant submits that the Examiner employs improper hindsight in asserting that the foregoing generic disclosures of the arguably non-analogous Mhalasakant reference renders the previous claims obvious. Specifically, MPEP § 2142 states that "impermissible hindsight must be avoided and the legal conclusion must be reached on the basis of the facts gleaned from the prior art" (emphasis added)." 'Any judgement on obviousness is in a sense necessarily a reconstruction based on hindsight reasoning, but so long as it takes into account only knowledge which was within the level of ordinary skill in the art at the time the claimed invention was made and does not include knowledge gleaned only from applicant's disclosure, such a reconstruction is proper'" (MPEP § 2145(X)(A), quoting In re McLaughlin, 443 F.2d 1392, 1395 (CCPA 1971), (emphasis added). Given the amendments to the claim, this would be even more so in making any such rejection with regard to alleging that the currently amended claim 1 is obvious over White in view of Mhalasakant.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). In this case, since the obviousness argument uses only knowledge of one of ordinary skill in the art and the teachings of the prior art, no impermissible hindsight was used.
Furthermore, the nonobviousness of the presently claimed invention is underscored by the lack of a reasonable expectation of success in achieving a stable liquid pharmaceutical formulation of the specific anti-PVRIG antibody as recited in the present claims. …. Here, it is widely recognized that the functional properties of protein formulations are heavily dependent on the specific interactions among the formulation components, including both the excipients and the active protein. Accordingly, Applicant respectfully submits that, given that "White does not teach the formulation according to claim l", and absent detailed guidance it would not have been reasonable to expect that one could apply Mhalasakant's generic teachings regarding histidine, arginine, polysorbate 80, NaCl, and pH to arrive at the stable liquid formulation of the particular anti-PVRIG antibody as recited in the presently amended claims.
In response to applicant's argument of lack of a reasonable expectation of success, in the field of biological technology, no invention has absolute certainty of success before experimental tests. Thus, only a reasonable expectation of success (not absolute) would have motivated an artisan to make the claimed fusion protein. As discussed above, Mhalasakant teaches a liquid formulation suitable for a wide range of antibodies. One of ordinary skill in the art would have had a reasonable expectation that the formulation would be suitable for the antibody of White. Given the teachings from references, an ordinary skilled in the art would have would have had a reasonable expectation of success in producing the claimed invention.
Lastly, Applicant argues that the claimed formulations provides surprising and unexpected results, in particular:
This formulation corresponds to formulation B4, one of 20 formulations (A1-A10 and B1-B10) analyzed by the inventors that revealed its superior features with regard to stability after agitation and storage under a variety of conditions.
Applicant mainly argues that formulation B4 provides unexpected superior results. However, the evidence of nonobviousness must be commensurate in scope with the claims to rebut the prima facie case of obviousness. See MPEP 716.02 (d). Thus the evidence provided with B4 is not sufficient to overcome the obviousness rejection because the claims are not limited to the formulation of B4. For example, the claims encompass formulations B9 and B10 (see Fig. 6 on page 19 of Remarks filed 05/14/2026). As acknowledged by Applicant, an additional acidic species was present in formulation B9 and B10. Thus, B9 and B10 were considered less useful than B4 (see paragraph 1 on page 20 of Remarks filed 05/14/2026).
Further, B4 is a formulation comprising specific amount of antibody and specific amount of the components (b) to (e), however, the claims encompass a wide ranges of each component in the formulation. Given that the superior results are only observed in B4, but not in B9 and B10, the superior results of formulation B4 may not be extended to other formulations encompassed by the claims with different concentrations from B4.
Thus, in view of the foregoing, when all of the evidence is considered, the totality of the rebuttal evidence of nonobviousness fails to outweigh the evidence of obviousness.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
U.S. Patent No. 10,227,408
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 10,227,408 B2 (hereinafter Pat. 408, corresponding to Appl. 15/048,967, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
Claims of Pat. 408 teaches:
1. A composition comprising an anti-PVRIG antibody, wherein said antibody comprises:
i) the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO:1434 and
ii) the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO:1453.
As shown below, SEQ ID NO: 1434 of Pat. 408 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim:
Query Match 26.6%; Score 634; DB 1; Length 120;
Best Local Similarity 100.0%;
Matches 120; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYNINWVRQAPGQGLEWMGYIYPYIGGSGY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYNINWVRQAPGQGLEWMGYIYPYIGGSGY 60
Qy 61 AQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCAREDKTARNAMDYWGQGTLVTVSS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCAREDKTARNAMDYWGQGTLVTVSS 120
SEQ ID NO: 1453 of Pat. 408 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim:
Query Match 50.6%; Score 566; DB 1; Length 107;
Best Local Similarity 100.0%;
Matches 107; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQMTQSPSSLSASVGDRVTITCRVSENIYSNLAWYQQKPGKAPKLLIYEATNLAEGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQMTQSPSSLSASVGDRVTITCRVSENIYSNLAWYQQKPGKAPKLLIYEATNLAEGVPS 60
Qy 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQHFWGTPYTFGQGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGTDFTLTISSLQPEDFATYYCQHFWGTPYTFGQGTKLEIK 107
2. A composition according to claim 1 wherein said antibody comprises the heavy chain variable domain of SEQ ID NO:1434 and the light chain variable domain of SEQ ID NO:1453.
3. A composition according to claim 1 wherein said antibody comprises a CH1-hinge-CH2-CH3 region from human IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. A composition according to claim 3 wherein said antibody comprises the CH1-hinge-CH2-CH3 region from human IgG4.
5. A composition according to claim 3 wherein said hinge region comprises mutations.
6. A composition according to claim 3 wherein said antibody comprises a CL region of human kappa 2 light chain.
Thus, the claims of Pat. 408 teach the antibodies of the instant claims 1-5, 22, 23, 26 and 36.
The claims of Pat. 408 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 408 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite full length heavy chain and light chain of antibody CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 408 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 9,714,289
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 9,714,289 B2 (hereinafter Pat. 289, corresponding to Appl. 15/277,978, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 15/277,978 (Pat. 289). Thus, Pat. 408 and Pat. 289 share the same disclosure, including the sequence listing.
Claims of Pat. 289 teaches:
1. A method of activating T-cells of a patient with cancer comprising administering an anti-PVRIG antibody to said patient, wherein said antibody comprises:
i) the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO:1434 and
ii) the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO:1453,
wherein a subset of said T-cells of said patient are activated.
2. A method according to claim 1 wherein said antibody comprises the heavy chain variable domain of SEQ ID NO:1434 and the light chain variable domain of SEQ ID NO:1453. As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim.
3. A method according to claim 2 wherein said antibody further comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. A method according to claim 2 wherein said antibody further comprises the CL region of human kappa 2 light chain.
Although the claims of Pat. 289 are drawn to a method, the claims of Pat. 289 teach the anti-PVRIG antibody which reads on the antibody of instant claims 1-5, 22, 23, 26 and 36, as set forth above (see rejection based on Pat. 408).
The claims of Pat. 289 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 289 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and full length light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 289 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 11,220,542
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-42 of U.S. Patent No. 11,220,542 B2 (hereinafter Pat. 542, corresponding to Appl. 15/277,980, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 15/277,980 (Pat. 542). Thus, Pat. 408 and Pat. 542 share the same disclosure, including the sequence listing.
The claims of Pat. 542 teach:
7. A method of activating T-cells of a patient with cancer comprising administering an anti-PVRIG antibody to said patient, wherein said anti-PVRIG antibody comprises:
i) a heavy chain variable domain comprising a sequence exhibiting at least 90% identity to SEQ ID NO:1434, wherein each individual vhCDR from SEQ ID NO:1434 comprises no more than 1 substitution, and wherein the vhCDR3 comprises no substitutions, and
ii) a light chain variable domain comprising a sequence exhibiting at least 90% identity to SEQ ID NO:1453, wherein each individual v1CDR from SEQ ID NO:1453 comprises no more than 1 substitution, and wherein the vlCDR3 comprises no substitutions, and
wherein a subset of said T-cells of said patient are activated.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim.
8. A method according to claim 7 wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
9. A method according to claim 7 wherein said anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
Although the claims of Pat. 542 are drawn to a method, the claims of Pat. 542 teach the anti-PVRIG antibody which reads on the antibody of instant claims 1-5, 22, 23, 26 and 36, as set forth above (see rejection based on Pat. 408).
The claims of Pat. 542 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 542 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and full length light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 542 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 10,351,625
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-34 of U.S. Patent No. 10,351,625 B2 (hereinafter Pat. 625, corresponding to Appl. 15/896,040, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 15/896,040 (Pat. 625). Thus, Pat. 408 and Pat. 625 share the same disclosure, including the sequence listing.
The claims of Pat. 625 teach:
1. A method of activating T-cells of a patient with cancer comprising administering an anti-PD-1 antibody and an anti-PVRIG antibody to said patient, wherein said anti-PVRIG antibody comprises:
i) a heavy chain variable domain comprising the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO:1434 and
ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO:1453, wherein a subset of said T-cells of said patient are activated.
2. A method according to claim 1 wherein said anti-PVRIG antibody comprises the heavy chain variable domain of SEQ ID NO:1434 and the light chain variable domain of SEQ ID NO:1453.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim.
3. A method according to claim 2 wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. A method according to claim 3 wherein said anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
Although the claims of Pat. 625 are drawn to a method, the claims of Pat. 625 teach the anti-PVRIG antibody which reads on the antibody of instant claims 1-5, 22, 23, 26 and 36, as set forth above (see rejection based on Pat. 408).
The claims of Pat. 625 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 625 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and full length light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 625 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 11,623,955
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-33 of U.S. Patent No. 11,623,955 B2 (hereinafter Pat. 955, corresponding to Appl. 16/748,695, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 16/748,695 (Pat. 955). Thus, Pat. 408 and Pat. 955 share the same disclosure, including the sequence listing.
The claims of Pat. 955 teach:
1. A method of activating NK-cells of a patient with cancer comprising administering an anti-PVRIG antibody to said patient, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO: 1434 and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO: 1453, wherein a subset of said NK-cells of said patient are activated.
2. A method according to claim 1 wherein said anti-PVRIG antibody comprises the heavy chain variable domain of SEQ ID NO: 1434 and the light chain variable domain of SEQ ID NO:1453.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim.
3. A method according to claim 2 wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. A method according to claim 3 wherein said anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
Although the claims of Pat. 955 are drawn to a method, the claims of Pat. 955 teach the anti-PVRIG antibody which reads on the antibody of instant claims 1-5, 22, 23, 26 and 36, as set forth above (see rejection based on Pat. 408).
The claims of Pat. 955 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 955 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and full length of light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 955 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 11,795,220
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. 11,795,220 B2 (hereinafter Pat. 220, corresponding to Appl. 16/904,510, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 16/904,510 (Pat. 220). Thus, Pat. 408 and Pat. 220 share the same disclosure, including the sequence listing.
The claims of Pat. 220 teach:
1. A method of activating T-cells of a patient with cancer comprising administering an anti-PD-L1 antibody and an anti-PVRIG antibody to said patient, wherein said anti-PVRIG antibody comprises:
i) a heavy chain variable domain comprising the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO:1434 and
ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO:1453,
wherein a subset of said T-cells of said patient are activated.
2. The method according to claim 1 wherein said anti-PVRIG antibody comprises the heavy chain variable domain of SEQ ID NO:1434 and the light chain variable domain of SEQ ID NO:1453.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim.
3. The method according to claim 2 wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. The method according to claim 3 wherein said anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
Although the claims of Pat. 220 are drawn to a method, the claims of Pat. 220 teach the anti-PVRIG antibody which reads on the antibody of instant claims 1-5, 22, 23, 26 and 36, as set forth above (see rejection based on Pat. 408).
The claims of Pat. 220 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 220 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 220 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 12,312,404
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 12,312,404 B2 (hereinafter Pat. 404, corresponding to Appl. 18/488,870) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 18/488,870 (Pat. 404). Thus, Pat. 408 and Pat. 404 share the same disclosure, including the sequence listing.
The claims of Appl. 870 teach:
1. A composition comprising an anti-PVRIG antibody, wherein the anti-PVRIG antibody specifically binds to human PVRIG, wherein the antibody comprises a heavy chain and a light chain, and wherein: a) the heavy chain comprises a heavy chain variable domain having at least 90% or at least 95% identity to the amino acid sequence of SEQ ID NO: 1434; and b) the light chain comprises a light chain variable domain having at least 90% or at least 95% identity to the amino acid sequence of SEQ ID NO: 1453.
7. The composition according to claim 1, wherein the anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein the hinge region optionally comprises one or more mutations.
8. The composition according to claim 44, wherein the anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim. Thus, the claims of Pat. 404 teach the antibodies of the instant claims 1-5, 22, 23, 26 and 36.
The claims of Pat. 404 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 404 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 404 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
Application No. 19/190,452
Claim 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 38-61 of copending Application No. 19/190,452 (hereinafter Appl. 452, US 2025/0333503 A1) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
It is noted that Appl. 15/048,967 (Pat. 408) is the parent application for Appl. 19/190,452 (Appl. 452). Thus, Pat. 408 and Appl. 452 share the same disclosure, including the sequence listing.
The claims of Appl. 452 teach:
38. A composition comprising an anti-PVRIG antibody that specifically binds to human PVRIG, wherein the anti-PVRIG antibody comprises:
a) the vhCDR1, vhCDR2, and vhCDR3 from SEQ ID NO: 1434, and
b) the vlCDR1, vlCDR2, and vlCDR3 from SEQ ID NO:1453;
wherein said CDRs comprise from 0 to 4 substitutions, and no individual CDR comprises more than 1 substitution, and wherein the vhCDR3 and vlCDR3 comprise no substitutions.
39. The composition according to claim 38, wherein said anti-PVRIG antibody comprises a heavy chain variable domain comprising a sequence exhibiting at least 90% identity to SEQ ID NO: 1434, and a light chain variable domain comprising a sequence exhibiting at least 90% identity to SEQ ID NO: 1453.
40. The composition according to claim 38, wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
41. The composition according to claim 38, wherein said anti-PVRIG antibody comprises the CL region of human kappa 2 light chain.
As set forth above (see rejection based on Pat. 408), SEQ ID NO: 1434 comprises the heavy chain variable region of SEQ ID NO: 8 of the instant claim; SEQ ID NO: 1453 comprises the heavy chain variable region of SEQ ID NO: 13 of the instant claim. Thus, the claims of Pat. 404 teach the antibodies of the instant claims 1-5, 22, 23, 26 and 36.
The claims of Appl. 452 teach the anti-PVRIG antibody as set forth above. However, the claims of Appl. 452 do not teach the formulation according to claim 1, or the antibodies of instant claims 25 and 27 which recite the full length heavy chain and light chain of CHA.7.518.1.H4 (S241P). White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) which reads on the antibodies of the instant claims 25 and 27. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Appl. 452 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 10,751,415
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-22 of U.S. Patent No. 10,751,415 B2 (hereinafter Pat. 415, corresponding to Appl. 15/680,187, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 415 teach:
7. A composition according to claim 5 wherein said second antibody binds human PVRIG (SEQ ID NO:2).
8. A composition according to claim 7 wherein said second antibody comprises an antigen binding domain comprising a variable heavy domain comprising SEQ ID NO:5 and a variable light domain comprising SEQ ID NO:10.
9. A composition according to claim 7 wherein the heavy chain of said second antibody has SEQ ID NO: 9 and the light chain of said second antibody has SEQ ID NO: 14.
As evidenced by the Fig. 3A of the specification of Pat. 415, SEQ ID NO: 9 and SEQ ID NO: 14 correspond to the heavy chain and the light chain of antibody: CHA.7.518.1.H4 (S241P). Thus, the claims of Pat. 415 teaches the antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
The claims of Pat. 415 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 173 do not teach the formulation according to claim 1, White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P). White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody comprising heavy chain of SEQ ID NO: 9 and light chain of SEQ ID NO: 14 as taught by the claims of Pat. 415 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 10,124,061
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 10,124,061 B2 (hereinafter Pat. 061, corresponding to Appl. 15/795,135, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 061 teach:
7. The method according to claim 5 wherein said second antibody binds human PVRIG extracellular domain (ECD) (SEQ ID NO:80).
8. The method according to claim 7 wherein said second antibody comprises an antigen binding domain comprising a variable heavy domain comprising SEQ ID NO:5 and a variable light domain comprising SEQ ID NO:10.
9. The method according to claim 7 wherein the heavy chain of said second antibody has SEQ ID NO:9 and the light chain of said second antibody has SEQ ID NO:14.
As evidenced by the Fig. 3A of the specification of Pat. 061, SEQ ID NO: 9 and SEQ ID NO: 14 correspond to the heavy chain and the light chain of antibody: CHA.7.518.1.H4 (S241P). Thus, the claims of Pat. 061 teaches the antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
Although the claims of Pat. 061 are drawn to a method, the claims of Pat. 061 also teach antibody used in the method, such as the anti-PVRIG antibody comprising the heavy chain of said second antibody has SEQ ID NO:9 and the light chain of said second antibody has SEQ ID NO:14.
The claims of Pat. 061 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 061 do not teach the formulation according to claim 1, White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P). White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody comprising heavy chain of SEQ ID NO: 9 and light chain of SEQ ID NO: 14 as taught by the claims of Pat. 061 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 10,213,505
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 of U.S. Patent No. 10,213,505 B2 (hereinafter Pat. 505, corresponding to Appl. 15/937,784, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 505 teach:
1. A composition comprising an anti-PVRIG antibody, wherein said antibody comprises: i) a heavy chain comprising SEQ ID NO:9, and ii) a light chain comprising SEQ ID NO:14.
As evidenced by the Fig. 3A of the specification of Pat. 505, SEQ ID NO: 9 and SEQ ID NO: 14 correspond to the heavy chain and the light chain of antibody: CHA.7.518.1.H4 (S241P). Thus, the claims of Pat. 505 teaches the antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
The claims of Pat. 505 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 505 do not teach the formulation according to claim 1, White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P). White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody comprising heavy chain of SEQ ID NO: 9 and light chain of SEQ ID NO: 14 as taught by the claims of Pat. 505 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 11,701,424
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of U.S. Patent No. 11,701,424 B2 (hereinafter Pat. 424, corresponding to Appl. 16/904,511, cited in IDS of 01/17/2025) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 424 teach:
1. A method of activating T-cells of a patient with cancer comprising administering an anti-PD-L1 antibody and an anti-PVRIG antibody to said patient, wherein said anti-PVRIG antibody comprises:
i) a heavy chain comprising SEQ ID NO: 9, and
ii) a light chain comprising SEQ ID NO: 14.
As evidenced by the Fig. 3A of the specification of Pat. 424, SEQ ID NO: 9 and SEQ ID NO: 14 correspond to the heavy chain and the light chain of antibody: CHA.7.518.1.H4 (S241P). Thus, the claims of Pat. 424 teaches the antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
Although the claims of Pat. 424 are drawn to a method, the claims of Pat. 424 also teach antibody used in the method, such as the anti-PVRIG antibody comprising the heavy chain of said second antibody has SEQ ID NO:9 and the light chain of said second antibody has SEQ ID NO:14.
The claims of Pat. 424 teach the anti-PVRIG antibody as set forth above. However, the claims of Pat. 424 do not teach the formulation according to claim 1. White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P). White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody comprising heavy chain of SEQ ID NO: 9 and light chain of SEQ ID NO: 14 as taught by the claims of Pat. 424 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 11,225,523
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 11,225,523 B2 (hereinafter Pat. 523, corresponding to Appl. 15/996,369, cited in IDS of 01/17/2025) in view of Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 523 teach:
1. A method of treatment for cancer in a patient comprising administering the triple combination comprising an anti-TIGIT antibody, an anti-PVRIG antibody and an anti-PD-1 antibody, wherein said anti-PVRIG antibody is an antibody chosen from at least one of CHA.7.518.1.H4(S241P) and CHA.7.538.1.2.H4(S241P). As set forth in the 103 rejection above, antibody CHA.7.518.1.H4 (S241P) reads on antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
10. The method of treatment according to claim 1, wherein said cancer is selected from the group consisting of ovarian cancer, triple negative breast cancer, stomach (gastric) cancer, lung cancer (small cell lung, non-small cell lung), Merkel Cells cancer, MSI-high cancer, KRAS mutant tumors, adult T-cell leukemia/lymphoma, and Myelodysplastic syndromes (MDS).
11. The method of treatment according to claim 1, wherein the antibodies are provided in an administration kit with dosage units of each antibody, either packaged separately in individual dosage units, or together, as a mixture of antibodies as a single dosage unit.
Although the claims of Pat. 523 are drawn to a method, the claims of Pat. 523 also teach antibody used in the method, such as CHA.7.518.1.H4 (S241P).
The claims of Pat. 523 teach the anti-PVRIG antibody and the method of treating various cancers with the antibody, as set forth above. However, the claims of Pat. 523 do not teach the formulation according to claim 1. Mhalasakant’s teachings are described above. In particular, Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 523, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by the claims of Pat. 523 and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
U.S. Patent No. 12,152,084
Claims 1-13, 16-23, 25-30, and 34-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-12 of U.S. Patent No. 12,152,084 B2 (hereinafter Pat. 04, corresponding to Appl. 17/544,852, cited in IDS of 01/17/2025) in view of Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Pat. 084 teach:
1. A method of treatment for cancer in a patient comprising administering the triple combination comprising an anti-TIGIT antibody, an anti-PVRIG antibody and an anti-PD-1 antibody, wherein said anti-TIGIT antibody is an antibody chosen from at least one of CPA.9.083.H4(S241P), CPA.9.086.H4(S241P), CHA.9.547.7.H4(S241P) and CHA.9.547.13.H4(S241P).
4. The method of treatment according to claim 1, wherein said anti-PVRIG antibody is an antibody chosen from at least one of CHA.7.518.1.H4 (S241P) and CHA.7.538.1.2.H4(S241P). As set forth in the 103 rejection above, antibody CHA.7.518.1.H4 (S241P) reads on antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36.
11. The method of treatment according to claim 1, wherein said cancer is selected from the group consisting of ovarian cancer, triple negative breast cancer, stomach (gastric) cancer, lung cancer (small cell lung, non-small cell lung), Merkel Cells cancer, MSI-high cancer, KRAS mutant tumors, adult T-cell leukemia/lymphoma, and Myelodysplastic syndromes (MDS).
12. The method of treatment according to claim 1, wherein the antibodies are provided in an administration kit with dosage units of each antibody, either packaged separately in individual dosage units, or together, as a mixture of antibodies as a single dosage unit.
Although the claims of Pat. 084 are drawn to a method, the claims of Pat. 084 also teach antibody used in the method, such as CHA.7.518.1.H4 (S241P).
The claims of Pat. 084 teach the anti-PVRIG antibody and the method of treating various cancers with the antibody, as set forth above. However, the claims of Pat. 084 do not teach the formulation according to claim 1. Mhalasakant’s teachings are described above. In particular, Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as such as CHA.7.518.1.H4 (S241P) as taught by the claims of Pat. 084, because the antibody can be used to treat various cancers in combination with other antibodies as taught by the claims of Pat. 084 and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
Application No. 18/774,872
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 59-73 of copending Application No. 18/774,872 (hereinafter Appl. 872, US 2025/0136710 A1) in view of Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Appl. 872 teach:
59. (New) A method of treatment for cancer in a patient comprising administering an anti-TIGIT antibody, an anti-PVRIG antibody, and either an anti-PD-1 antibody or an anti-PD-L1 antibody; wherein the anti-TIGIT antibody comprises:(i) a heavy variable domain having at least about 75% or at least about 80% sequence identity to a heavy chain variable domain from an anti-TIGIT antibody selected from the group consisting of CPA.9.083.H4(S241P), CPA.9.086.H4(S241P), CHA.9.547.7.H4(S241P) and CHA.9.547.13.H4(S241P); and (ii) a light variable domain having at least about 75% or at least about 80% sequence identity to a light chain variable domain from the anti-TIGIT antibody in (i)
62. (New) The method of claim 59, wherein the anti-PVRIG antibody comprises:(i) a heavy variable domain having at least about 75% or at least about 80% sequence identity to a heavy chain variable domain from an anti-PVRIG antibody selected from the group consisting of CHA.7.518.1.H4(S241P) and CHA.7.538.1.2.H4(S241P); and (ii) a light variable domain having at least about 75% or at least about 80% sequence identity to a light chain variable domain from the anti-PVRIG antibody in (i).
64. (New) The method of claim 62, wherein the anti-PVRIG antibody comprises:(i) a heavy variable domain having at least about 90% sequence identity to the heavy chain variable domain from an anti-PVRIG antibody selected from the group consisting of CHA.7.518.1.H4(S241P) and CHA.7.538.1.2.H4(S241P); and (ii) a light variable domain having at least about 90% sequence identity to the light chain variable domain from the anti-PVRIG antibody in (i). As set forth in the 103 rejection above, antibody CHA.7.518.1.H4 (S241P) reads on antibodies of instant claims 1-5, 22, 23, 25, 26 and 27.
72. (New) The method of claim 59, wherein the cancer is selected from the group consisting of ovarian cancer, triple negative breast cancer,…, and Myelodysplastic syndromes (MDS).
Although the claims of Appl. 872 are drawn to a method, the claims of Appl. 872 also teach antibody used in the method, such as CHA.7.518.1.H4 (S241P).
The claims of Appl. 872 teach the anti-PVRIG antibody and the method of treating various cancers with the antibody, as set forth above. However, the claims of Appl. 872 do not teach the formulation according to claim 1. Mhalasakant’s teachings are described above. In particular, Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as such as CHA.7.518.1.H4 (S241P) as taught by the claims of Appl. 872, because the antibody can be used to treat various cancers in combination with other antibodies as taught by the claims of Appl. 872 and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
Application No. 17/773,791
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5, 7, 9, 11, 13-23, and 25-32 of copending Application No. 17/773,791 (hereinafter Appl. 791, US 2022/0378742 A1).
Regarding instant claim 1, the claim 1 of Appl. 791 teaches a method of treatment for cancer comprising administering nivolumab and an anti-PVRIG antibody, wherein said anti-PVRIG antibody is administered as a stable liquid pharmaceutical formulation and, wherein the stable liquid pharmaceutical formulation of the anti-PVRIG antibody comprises:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9);(b) from 15 mM to 70 mM histidine; (c) from 30 mM to 90 mM NaCl; (d) from 50 mM to 120 mM L-Arginine; and (e) from 0.005% to 0.09% w/v polysorbate 80, wherein the composition has a pH from 6.3 to 6.8, and wherein the anti-PVRIG antibody is at a concentration of from 10 mg/mL to 40 mg/mL. Although claim 1 of Appl. 791 is drawn to a method, the claim teaches using a composition which read on the stable liquid pharmaceutical formulation, because claim 1 of Appl. 791 disclose the same antibody as the instant claim 1. The ranges of each component are within the ranges of the instant claim 1. It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to make the pharmaceutical formulation for the claimed method.
2. (Currently amended) The method of treatment according to any one of claim 1, wherein said anti-PVRIG antibody comprises a CH1-hinge-CH2-CH3 sequence of IgG4 (SEQ ID NO:17 or SEQ ID NO:50), wherein said hinge region optionally comprises mutations.
3. (Currently amended) The method of treatment according to claims 1, wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgGI, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations.
4. (Currently amended) The method of treatment according to claim 1, wherein said heavy chain variable domain is from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and said light chain variable domain is from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9).
5. (Previously presented) The method of treatment according to claim 1, wherein said anti- PVRIG antibody comprises a CL region of human kappa 2 light chain.
25. (Currently amended) The method of treatment according to claim 1, wherein said anti- PVRIG antibody formulation comprises: i) a heavy chain from CHA.7.518.1.H4 (S241P) (SEQ ID NO:8); and ii) a light chain from CHA.7.518.1.H4 (S241P) (SEQ ID NO:13).
Taken together, the claims of Appl. 791 disclose heavy chain and light chain of antibody CHA.7.518.1.H4 (S241P), which would read the antibodies of instant claims 1-5, 22, 23, 25, 26, 27 and 36 as set forth above (also see 103 rejection above).
Regarding the instant claims 6 and 7, claim 7 of Appl. 791 teaches wherein said pharmaceutical formulation comprises about 25 mM histidine.
Regarding the instant claims 8 and 9, claim 9 of Appl. 791 teaches wherein said pharmaceutical formulation comprises about 60 mM NaCl.
Regarding the instant claims 10 and 11, claim 11 of Appl. 791 teaches wherein said pharmaceutical formulation comprises about 100 mM L-arginine.
Regarding the instant claims 12 and 13, claim 13 of Appl. 791 teaches wherein said pharmaceutical formulation comprises about 0.01% polysorbate 80.
Regarding the instant claims 16, claims 14-16 of Appl. 791 teach wherein said pH is from 6 to 7.0 (claim 14); wherein said pH is from 6.3 to 6.8 (claim 15); wherein said pH is 6.5 +/- 0.2 (claim 16). It would have prima facie been obvious to one of ordinarily skilled in the art to make a pharmaceutical solution with a pH of 6.5, because it is the central pH value taught by the claim of Appl. 791.
Regarding the instant claim 17, claim 17 of Appl. 791 teaches wherein said anti- PVRIG antibody is at a concentration of from 15 mg/mL to 40 mg/mL, 15 mg/mL to 30 mg/mL, 10 mg/mL to 25 mg/mL, or 15 mg/mL to 25 mg/mL.
Regarding the instant claims 18-20, 34 and 35, claims 18-20 of Appl. 791 teach wherein said formulation is stable at 2°C to 8°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 8 weeks, 9 weeks, or 10 weeks (claim 18); wherein said formulation is stable at about 20°C to 25 °C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, or 6 weeks (claim 19); wherein said formulation is stable at 35°C to 40°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, or 5 weeks (claim 20).
Regarding the instant claim 21, claim 21 of Appl. 791 teaches wherein said anti- PVRIG antibody is at a concentration of about 20 mg/mL.
Regarding the instant claims 22 and 23, claims 22 and 23 of Appl. 791 teach wherein said anti- PVRIG antibody formulation comprises: a) a heavy chain comprising: i) a VH-CH1-hinge-CH2-CH3, wherein the VH is from CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and wherein the CH1-hinge- CH2-CH3 region is from IgG4; and b) a light chain comprising: i) a VL-CL, wherein the VL from CHA.7.518.1.H4(S241P) (SEQ ID NO:9) and wherein the CL region is from human kappa 2 light chain (claim 22); wherein said hinge region optionally comprises mutations (claim 23).
Regarding the instant claims 25-27 and 36, claims 26 and 27 of Appl. 791 teach said anti-PVRIG antibody formulation comprising: (a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) about 25 mM histidine; (c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and (e) about 0.01% w/v polysorbate 80, wherein the composition has a pH from 6.5 +/- 0.2 (claim 26); wherein said anti-PVRIG antibody comprises: i) a heavy chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:8); and ii) a light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13); (b) about 25 mM histidine; (c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and (e) about 0.01% w/v polysorbate 80, wherein the composition has a pH from 6.5 +/- 0.2.
Regarding the instant claims 28-30, claims 28-30 of Appl. 791 teach wherein said anti- PVRIG antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti- PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti-PVRIG antibody (claim 28); wherein said anti- PVRIG antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti- PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti-PVRIG antibody (claim 29); wherein said anti- PVRIG antibody is administered 20 mg/kg every 4 weeks (claim 31).
Although the claims of Appl. 791 are drawn to a method, the claims disclose the pharmaceutical formulation as set forth above. One of ordinary skill in the art would have known to make the pharmaceutical formulation in order to perform the method of treatment of Appl. 791, thus reaches the instantly claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Application No. 18/247,245
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-9, 11, 13, 15, 17, 20-26, and 28-34 of copending Application No. 18/247,245 (hereinafter Appl. 245, US 2023/0365680 A1).
Regarding the instant claim 1, claims 1 and 20 of Appl. 245 teach a method of treatment for cancer comprising administering BMS-986207, Nivolumab, and an anti-PVRIG antibody, wherein said anti-PVRIG antibody is administered as a stable liquid pharmaceutical formulation and, wherein the stable liquid pharmaceutical formulation of the anti-PVRIG antibody comprises:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) from 10 mM to 100 mM histidine; (c) from 30 mM to 100 mM NaCl; (d) from 20 mM to 150 mM L-Arginine; and (e) from 0.005% to 0.1% w/v polysorbate 80, wherein the formulation has a pH from 5.5 to 7.0 (claim 1); wherein the anti-PVRIG antibody is at a concentration of from 10 mg/ml to 40 mg/ml (claim 20). Although claims of Appl. 245 is drawn to a method, the claims teaches using a composition which read on the stable liquid pharmaceutical formulation, because claim 1 of Appl. 245 disclose the same antibody as the instant claim 1. The ranges of each component are within the ranges of the instant claims 1 and 20. It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to make the pharmaceutical formulation for the claimed method.
Regarding the instant claims 2-5, claims 5-8 of Appl. 245 teach wherein said anti-PVRIG antibody comprises a CH1-hinge-CH2-CH3 sequence of IgG4 (SEQ ID NO:17 or SEQ ID NO:50), wherein said hinge region optionally comprises mutations (claim 5); wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgG1, IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations (claim 6); wherein said heavy chain variable domain is from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and said light chain variable domain is from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9) (claim 7); wherein said anti-PVRIG antibody comprises a CL region of human kappa 2 light chain (claim 8).
Regarding the instant claims 6 and 7, claim 9 of Appl. 245 teaches wherein said pharmaceutical formulation comprises from 10 mM to 80 mM histidine, from 15 mM to 70 mM histidine, from 20 mM to 60 mM histidine, from 20 mM to 50 mM histidine, or from 20 mM to 30 mM histidine. The range of about 25 mM histidine (instant claim 7) overlaps with the range from 20 mM to 50 mM histidine.
Regarding the instant claims 8 and 9, claim 11 of Appl. 245 teaches wherein said pharmaceutical formulation comprises from 30 mM to 100 mM NaCl, from 30 mM to 90 mM NaCl, from 40 mM to 80 mM NaCl, or from 45 mM to 70 mM NaCl. The range of about 60 mM NaCl (instant claim 9) overlaps with the range of 45 mM to 70 mM NaCl.
Regarding the instant claims 10 and 11, claim 13 of Appl. 245 teaches wherein said pharmaceutical formulation comprises from 20 mM to 140 mM L-arginine, from 30 mM to 140 mM L-arginine, from 40 mM to 130 mM L-arginine, from 50 mM to 120 mM L- arginine, from 60 mM to 110 mM L-arginine, from 70 mM to 110 mM L-arginine, from 80 mM to 110 mM L-arginine, or from 90 mM to 110 mM L-arginine. The range of about 100 mM L-arginine (instant claim 11) overlaps with the range 90 mM to 110 mM L-arginine.
Regarding the instant claims 12 and 13, claim 15 of Appl. 245 teach wherein said pharmaceutical formulation comprises from 0.006% to 0.1% w/v polysorbate 80,from 0.007% to 0.09% w/v polysorbate 80, from 0.008% to 0.08% w/v polysorbate 80, from 0.009% to 0.09% w/v polysorbate 80, from 0.01% to 0.08% w/v polysorbate 80, from 0.01% to 0.07% w/v polysorbate 80, from 0.01% to 0.07% w/v polysorbate 80, or from 0.01% to 0.06% w/v polysorbate 80, or from 0.009% to 0.05% w/v polysorbate 80. The range of about 0.01% polysorbate 80 (instant claim 13) overlaps with the range 0.009% to 0.05% polysorbate.
Regarding the instant claim 16, claim 17 of Appl. 245 teaches wherein said pH is from 6 to 7.0, from 6.3 to 6.8, or 6.5+/- 0.2. It would have prima facie been obvious to one of ordinarily skilled in the art to make a pharmaceutical solution with a pH of 6.5, because it is the central pH value taught by the claim of Appl. 245.
Regarding the instant claims 17, claim 20 of Appl. 245 teaches wherein said anti-PVRIG antibody is at a concentration of from 10 mg/mL to 40 mg/mL, 15 mg/mL to 40 mg/mL, 15 mg/mL to 30 mg/mL, 10 mg/mL to 25 mg/mL, or 15 mg/mL to 25 mg/mL.
Regarding the instant claims 18-20, claims 21-23 of Appl. 245 teach wherein said formulation is stable at 2°C to 8°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 8 weeks, 9 weeks, or 10 weeks (claim 21); wherein said formulation is stable at about 20°C to 25 °C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, or 6 weeks (claim 22); wherein said formulation is stable at 35°C to 40°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, or 5 weeks (claim 23).
Regarding the instant claims 21, claim 24 of Appl. 245 teaches wherein said anti-PVRIG antibody is at a concentration of about 20 mg/mL.
Regarding the instant claims 22, claim 25 of Appl. 245 teaches wherein said anti-PVRIG antibody formulation comprises: a) a heavy chain comprising: i) a VH-CH1-hinge-CH2-CH3, wherein the VH is from CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and wherein the CH1-hinge-CH2- CH3 region is from IgG4; and b) a light chain comprising: i) a VL-CL, wherein the VL from CHA.7.518.1.H4(S241P) (SEQ ID NO:9) and wherein the CL region is from human kappa 2 light chain.
Regarding the instant claims 23, claim 26 of Appl. 245 teaches wherein said hinge region comprises mutations.
Regarding the instant claims 25, claim 28 of Appl. 245 teaches wherein said anti-PVRIG antibody formulation comprises: i) a heavy chain comprising the heavy chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:8); and ii) a light chain comprising the light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13).
Regarding the instant claims 26, claim 29 of Appl. 245 teaches said anti-PVRIG antibody formulation comprising:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and DB2/ 46768578.2 - 5 - ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) about 25 mM histidine; (c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and (e) about 0.01%% w/v polysorbate 80, wherein the formulation has a pH from 6.5 +/- 0.2
Regarding the instant claims 27 and 36, claim 30 of Appl. 245 teaches said anti-PVRIG antibody formulation comprising:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain comprising the heavy chain from CHA.7.518.1.H4 (S241P) (SEQ ID NO:8); and ii) a light chain comprising the light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13); (b) about 25 mM histidine; (c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and (e) about 0.01%% w/v polysorbate 80, wherein the formulation has a pH from 6.5 +/- 0.2. claim 24 of Appl. 245 teaches wherein said anti-PVRIG antibody is at a concentration of about 20 mg/mL.
Regarding the instant claims 28-30, claims 31, 32 and 34 of Appl. 245 teach wherein said anti-PVRIG antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti-PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti-PVRIG antibody or about 10 mg/kg to about 20 mg/kg of the anti-PVRIG antibody (claim 31); wherein said anti-PVRIG antibody is administered at a dosage of about 0.01 mg/kg, 0.03 mg/kg,0.1 mg/kg, 0.3 mg/kg, 1 mg/kg, 3 mg/kg, 10 mg/kg, or 20 mg/kg of the anti-PVRIG antibody (claim 32); wherein said anti-PVRIG antibody is administered 20 mg/kg every 4 weeks (claim 34).
Although the claims of Appl. 245 are drawn to a method, the claims disclose the pharmaceutical formulation as set forth above. One of ordinary skill in the art would have known to make the pharmaceutical formulation in order to perform the method of treatment of Appl. 791, thus reaches the instantly claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Application No. 18/263,172
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/263,172 (hereinafter Appl. 172, US 2024/0076373 A1) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
Claim 1 of Appl. 172 teaches a method of treatment for cancer comprising administering nivolumab and an anti-PVRIG antibody, wherein said anti-PVRIG antibody is administered as a stable liquid pharmaceutical formulation and, wherein the stable liquid pharmaceutical formulation of the anti-PVRIG antibody comprises:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) from 10 mM to 100 mM histidine; (c) from 30 mM to 100 mM NaCl; (d) from 20 mM to 150 mM L-Arginine; and (e) from 0.005% to 0.1% w/v polysorbate 80, wherein the formulation has a pH from 5.5 to 7.0. As evidenced by Fig. 3A of the specification of Appl. 172, SEQ ID NO: 4 and SEQ ID NO: 9 correspond to variable heavy (VH) domain and variable light (VL) domain of CHA.7.518.1.H4 (S241P), respectively. Thus, the claims of Appl. 172 teach antibodies which would read on the antibodies of the instant claims 1, 4, and 26.
Although claim 1 of Appl. 172 is drawn to a method, the claim teaches using a composition which read on the stable liquid pharmaceutical formulation, because claim 1 of Appl. 172 disclose the same antibody as the instant claim 1. The ranges of each component are the same as the ranges of the instant claim 1. It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to make the pharmaceutical formulation for the claimed method.
However, the claims of Appl. 172 do not teach the constant region of heavy chain and light chain, or full length heavy chain and light chain, or antibody concentration as instantly claimed.
White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) including full length heavy chain and full length light chain. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims, including antibody concentration. In particular, the range of 1-100 mg/ml taught by Mhalasakant (claim 69) and 10 mg/mL, or 25mg/mL or 50 mg/mL antibody concentration (Example 3) overlaps with the range 10 mg/mL to 40 mg/mL of instant claim 17, and the range about 20 mg/mL of instant claim 21.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Appl. 172 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Application No. 18/263,171
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/263,171 (hereinafter Appl. 171, US 2024/0082397 A1) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
Claim 1 of Appl. 171 teaches a stable liquid pharmaceutical formulation of an anti-PVRIG antibody comprising:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) from 10 mM to 100 mM histidine; (c) from 30 mM to 100 mM NaCl; (d) from 20 mM to 150 mM L-Arginine; and (e) from 0.005% to 0.1% w/v polysorbate 80, wherein the formulation has a pH from 5.5 to 7.0.
As evidenced by Fig. 3A of the specification of Appl. 171, SEQ ID NO: 4 and SEQ ID NO: 9 correspond to variable heavy (VH) domain and variable light (VL) domain of CHA.7.518.1.H4 (S241P), respectively. Thus, the claims of Appl. 171 teach antibodies which would read on the antibodies of the instant claims 1, 4, and 26. The ranges of each component overlap the ranges of the instant claim 1.
The claims of Appl. 171 teach the stable liquid pharmaceutical formulation of instant claim 1 as set forth above. However, the claims of Appl. 171 do not teach the constant region of heavy chain and light chain, or full length heavy chain and light chain, or antibody concentration as instantly claimed.
White and Mhalasakant’s teachings are described above. In particular, White teaches antibody: CHA.7.518.1.H4 (S241P) including full length heavy chain and full length light chain. White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims, including antibody concentration. In particular, the range of 1-100 mg/ml taught by Mhalasakant (claim 69) and 10 mg/mL, or 25mg/mL or 50 mg/mL antibody concentration (Example 3) overlaps with the range 10 mg/mL to 40 mg/mL of instant claim 17, and the range about 20 mg/mL of instant claim 21.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Appl. 171 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Application No. 18/185,632
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7, 12, 16, 18, 19, 23, 47, 48, 63, 65, 71, 73, and 196 of copending Application No. 18/185,632 (hereinafter Appl. 632, US 2024/0103010 A1).
The claims of Appl. 632 teach:
1. A method for determining a cancer patient population for treatment with an anti-PVRIG antibody, the method comprising:
(a) detecting the presence …, and/or DC2 that express PVRL2,
(b) quantitating the measurement …, and/or DC2 that express PVRL2; and
(c) treating the cancer patient with the anti-PVRIG antibody when one or more cellular components in (a) as quantitated in step (b) are present at an increased level as compared to a control or a patient that does not have detectable levels of the cells.
16. The method according to claim 1, wherein the anti-PVRIG treatment antibody comprises a heavy chain variable domain from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:8) and a light chain variable domain from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:13). As evidenced by Fig. 3A of the specification of Appl. 632, SEQ ID NO: 8 and SEQ ID NO: 13 correspond to full length heavy chain and full length light chain of CHA.7.518.1.H4(S241P), respectively.
48. The method according to claim 1, wherein the anti-PVRIG treatment antibody comprises a CH1-hinge-CH2-CH3 sequence of IgG4 (SEQ ID NO: 657 or SEQ ID NO: 658), wherein the hinge region optionally comprises mutations.
65. The method according to claim 47, wherein the anti-PVRIG antibody formulation comprises:
a) a heavy chain comprising: i) a VH-CH1-hinge-CH2-CH3, wherein the VH is from CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and wherein the CH1-hinge-CH2-CH3 region is from IgG4; and
b) a light chain comprising: i) a VL-CL, wherein the VL is from CHA.7.518.1.H4(S241P) (SEQ ID NO:9) and wherein the CL region is from human kappa 2 light chain.
Although the claims of Appl. 632 are drawn to a method, the claims of Appl. 632 teach the full length heavy chain and light chain of anti-PVRIG antibody: CHA.7.518.1.H4 (S241P) which reads on the antibody of instant claims 1-5, 22, 23, 25, 26, 27 and 36, as set forth above (see 103 rejection set forth above).
47. The method according to claim 1, wherein the anti-PVRIG treatment antibody is administered as a stable liquid pharmaceutical formulation of the anti-PVRIG antibody comprising:
(a) an anti-PVRIG antibody, wherein the anti-PVRIG antibody comprises:
i) a heavy chain variable domain comprising the vhCDR1, vhCDR2, and vhCDR3 from the heavy chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:8), and
ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain of CHA.7.518.1.H4(S241P) (SEQ ID NO:13);
(b) from 10 mM to 100 mM histidine;
(c) from 30 mM to 100 mM NaCl;
(d) from 20 mM to 150 mM L-Arginine; and
(e) from 0.005% to 0.1% w/v polysorbate 80,
wherein the formulation has a pH from 5.5 to 7.0.
63. The method according to claim 47, wherein the anti-PVRIG antibody is at a concentration of from 10 mg/mL to 40 mg/mL, 15 mg/mL to 40 mg/mL, 15 mg/mL to 30 mg/mL, 10 mg/mL to 25 mg/mL, or 15 mg/mL to 25 mg/mL. The range about 20 mg/ml overlaps with the range of 10 mg/ml to 25 mg/ml.
Taken together, the claims of Appl. 632 teach a stable liquid pharmaceutical formulation would read on the instant claims 1-14, 16, 26, 27, and 36 because the ranges in claim 47 of Appl. 632 overlaps with the ranges recited by the instant claims 1-14, 16, 26, 27 and 36. It is also noted that optimum suitable ranges may be obtained by routine experimentation, absent a showing of criticality or unexpected results. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05(II)(A).
Regarding the instant claims 17 and 21, claim 63 of Appl. 632 The method according to claim 47, wherein the anti-PVRIG antibody is at a concentration of from 10 mg/mL to 40 mg/mL, 15 mg/mL to 40 mg/mL, 15 mg/mL to 30 mg/mL, 10 mg/mL to 25 mg/mL, or 15 mg/mL to 25 mg/mL. The range about 20 mg/ml overlaps with the range of 10 mg/ml to 25 mg/ml.
Regarding claims 18-20, 34 and 35, the “stable” properties recited are merely intended results of the method steps positively recited. The court noted (quoting Minton v. Nat'/ Ass'n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a "'whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited."' Id. Therefore, the stable properties of claims 18-20, 34 and 35 are given no weight. Since the claims of Appl. 632 teach the same pharmaceutical formulation, the same pharmaceutical formulation would have same physical and chemical properties (including stability) as claimed.
Regarding the instant claims 28-30, claim 71 and 73 teach wherein the anti-PVRIG treatment antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti-PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti-PVRIG antibody (claim 71); wherein the anti-PVRIG treatment antibody is administered 20 mg/kg every 4 weeks (claim 73).
Although the claims of Appl. 632 are drawn to a method, the claims disclose the pharmaceutical formulation as set forth above. One of ordinary skill in the art would have known to make the pharmaceutical formulation in order to perform the method of treatment of Appl. 632, thus reaches the instantly claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Application No. 18/754,029
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 31, 56, 81 of copending Application No. 18/754,029 (hereinafter Appl. 029, US 2024/0425607 A1) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Appl. 029 teach:
31. A method of treating cancer in a patient, comprising administering a composition comprising an anti-IL18-BP antibody, wherein said anti-IL18-BP antibody activates T cells, NK cells, NKT cells, Dendritic cells, MAIT T cells, 76 T cells, and/or innate lymphoid cells (ILCs), and/or modulates Myeloid cells, thereby said cancer is treated, optionally wherein (i) the T-cell is cytotoxic T-cell (CTL); optionally wherein the T-cell is CD4+ T-cell or CD8+ T-cell; or (ii) the NK-cell is CD16+ lymphocyte or CD56+NK cell.
56. The method of claim 31, further comprising administering a second antibody,
optionally wherein the second antibody is an antibody that binds to and/or inhibits a human checkpoint receptor protein; optionally wherein the second antibody is selected from the group consisting of an anti-PVRIG antibody,… or optionally wherein: (I) the PVRIG antibody (i) is selected from the group consisting of CHA.7.518.1.H4 (S241P) and CHA.7.538.1.2.H4(S241P) (claim 56).
81. The method of claim 31, wherein said cancer is selected from the group consisting of renal clear cell carcinoma (RCC), lung cancer, NSCLC, lung adenocarcinoma, lung squamous cell carcinoma, gastric adenocarcinoma, ovarian cancer, endometrial cancer, breast cancer, triple negative breast cancer (TNBC), head and neck tumor, colorectal adenocarcinoma, melanoma, colon cancer, glioblastoma multiforme, pancreatic adenocarcinoma, skin cutaneous melanoma, stomach adenocarcinoma and metastatic melanoma.
Although the claims of Appl. 029 are drawn to a method, the claims of Appl. 029 teach the full length heavy chain and light chain of anti-PVRIG antibody: CHA.7.518.1.H4 (S241P) which reads on the antibody of instant claims 1-5, 22, 23, 25, 26, 27 and 36, as set forth above (see 103 rejection set forth above).
The claims of Appl. 029 teach the anti-PVRIG antibody as set forth above. However, the claims of Appl. 029 do not teach the formulation according to claim 1 or other depended claims. White and Mhalasakant’s teachings are described above (see 103 rejection). In particular, White teaches antibody: CHA.7.518.1.H4 (S241P). White also teaches the antibody can be used in treating cancers. Mhalasakant teaches the formulation ranges of each components are overlapping with the ranges recited by instant claims.
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to produce anti-PVRIG antibody such as CHA.7.518.1.H4 (S241P) as taught by the claims of Appl. 029 and White, because the antibody can be used to treat various cancers alone or in combination with other antibodies as taught by the claims of Appl. 029 and White and to make a pharmaceutical composition comprising the antibody in a formulation taught by Mhalasakant with a reasonable expectation of success, because antibodies in the formulation are stable under various temperature conditions, as taught by Mhalasakant. The motivation is to make a pharmaceutical formulation to maintain activity of the antibody: CHA.7.518.1.H4 (S241P).
Application No. 18/700,194
Claims 1-13, 16-23, 25-30, and 34-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 4, 5, 7-9, 11-16, 19-22, 24, 26, 28, 30, 33-43, 45-49, 51, 53, 55, 74 and 75 of copending Application No. 18/700,194 (hereinafter Appl. 194, US 2025/0339522 A1) in view of White (White et al., WO 2018/033798 A1, Publication Date: 02/22/2018, cited in IDS of 01/17/2025, of record) and Mhalasakant (Mhalasakant et al., WO 2018/116198 A1, Publication Date: 06/28/2018, cited in IDS of 01/17/2025, of record).
The claims of Appl. 194 teach:
1. (Currently amended) A method of treatment for cancer by blocking DNAM axis in a patient in need thereof, the method comprising administering BMS-986207, Nivolumab, and an anti- poliovirus receptor related immunoglobulin domain containing (anti-PVRIG) antibody, wherein said anti-PVRIG antibody is administered as a stable liquid pharmaceutical formulation and, wherein the stable liquid pharmaceutical formulation of the anti-PVRIG antibody comprises:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9); (b) from 10 mM to 100 mM histidine; (c) from 30 mM to 100 mM NaCl; (d) from 20 mM to 150 mM L-Arginine; and (e) from 0.005% to 0.1% w/v polysorbate 80, wherein the composition has a pH from 5.5 to 7.0.
33. The method of treatment according to claim 1, wherein said anti-PVRIG antibody is at a concentration of from 10 mg/ml to 40 mg/ml.
19. (Currently amended) The method of treatment according to claim 1, wherein said anti-PVRIG antibody comprises the CH1-hinge-CH2-CH3 region from IgGI,IgG2, IgG3, or IgG4, wherein said hinge region optionally comprises mutations; or wherein said anti-PVRIG antibody comprises a CH1-hinge-CH2-CH3 sequence of IgG4 (SEQ ID NO:17 or SEQ ID NO:56).
20. (Currently amended) The method of treatment according to claim 1 wherein said heavy chain variable domain is from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and said light chain variable domain is from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9).
21. (Currently amended) The method of treatment according to claim 1 wherein said anti-PVRIG antibody comprises a CL region of human kappa 2 light chain.
40. (Currently amended) The method of treatment according to claim 1, wherein said anti-PVRIG antibody formulation comprises: i) a heavy chain comprising the heavy chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:8); and ii) a light chain comprising the light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13). Thus, the claims of Appl. 194 teach full length heavy chain and full length light chain of antibody CHA.7.518.1.H4 (S241P). As set forth in the 103 rejection, antibody CHA.7.518.1.H4 (S241P) reads on the antibodies of the instant claims 1-5, 22, 23, 25, 26 and 27.
Although claims of Appl. 194 is drawn to a method. The claims disclose a stable liquid pharmaceutical formulation which would read on the instant claim 1.
Regarding the instant claims 6 and 7, claim 22 of Appl. 194 teaches wherein said pharmaceutical formulation comprises from 10 mM to 80 mM histidine, from 15 mM to 70 mM histidine, from 20 mM to 60 mM histidine, from 20 mM to 50 mM histidine, or from 20 mM to 30 mM histidine, or about 25 mM histidine.
Regarding the instant claims 8 and 9, claim 24 of Appl. 194 teaches wherein said pharmaceutical formulation comprises from 30 mM to 100 mM NaCl, from 30 mM to 90 mM NaCl, from 40 mM to 80 mM NaCl, from 30 mM to 70 mM histidine, from 45 mM to 70 mM NaCl, or about 60 mM NaCl.
Regarding the instant claims 10 and 11, claim 26 of Appl. 194 teaches wherein said pharmaceutical formulation comprises from 20 mM to 140 mM L-arginine, from 30 mM to 140 mM L-arginine, from 40 mM to 130 mM L-arginine, from 50 mM to 120 mM L-arginine, from 60 mM to 110 mM L-arginine, from 70 mM to 110 mM L-arginine, from 80 mM to 110 mM L-arginine, from 90 mM to 110 mM L-arginine, or about 100 mM L-arginine.
Regarding the instant claims 12 and 13, claim 28 of Appl. 194 teach wherein said pharmaceutical formulation comprises from 0.006% to 0.1% w/v polysorbate 80, from 0.007% to 0.09% w/v polysorbate 80, from 0.008% to 0.08% w/v polysorbate 80, from 0.009% to 0.09% w/v polysorbate 80, from 0.01% to 0.08% w/v polysorbate 80, from 0.01% to 0.07% w/v polysorbate 80, from 0.01% to 0.07% w/v polysorbate 80, or from 0.01% to 0.06% w/v polysorbate 80, or from 0.009% to 0.05% w/v polysorbate 80, or about 0.01% w/v polysorbate 80.
Regarding the instant claims 16, claim 30 of Appl. 194 teaches wherein said pH is from 6 to 7.0, from 6.3 to 6.8, or 6.5+/- 0.2.
Regarding the instant claims 17, claim 33 of Appl. 194 teaches wherein said anti-PVRIG antibody is at a concentration of from 10 mg/mL to 40 mg/mL, 15 mg/mL to 40 mg/mL, 15 mg/mL to 30 mg/mL, 10 mg/mL to 25 mg/mL, or 15 mg/mL to 25 mg/mL.
Regarding the instant claims 18-20, 34 and 35, claims 34-36 of Appl. 194 teach wherein said formulation is stable at 2°C to 8°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 8 weeks, 9 weeks, or 10 weeks (claim 34); wherein said formulation is stable at about 20°C to 25 °C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, or 6 weeks (claim 35); wherein said formulation is stable at 35°C to 40°C for at least 1 week, 2 weeks, 3 weeks, 4 weeks, or 5 weeks (claim 36).
Regarding the instant claims 21, claim 37 of Appl. 194 teaches wherein said anti-PVRIG antibody is at a concentration of about 20 mg/mL.
Regarding the instant claims 22, claim 38 of Appl. 194 teaches wherein said anti-PVRIG antibody formulation comprises: a) a heavy chain comprising: i) a VH-CH1-hinge-CH2-CH3, wherein the VH is from CHA.7.518.1.H4(S241P) (SEQ ID NO:4) and wherein the CH1-hinge-CH2- CH3 region is from IgG4; and b) a light chain comprising: i) a VL-CL, wherein the VL from CHA.7.518.1.H4(S241P) (SEQ ID NO:9) and wherein the CL region is from human kappa 2 light chain.
Regarding the instant claims 23, claim 39 of Appl. 194 teaches wherein said hinge region comprises mutations.
Regarding the instant claims 25, claim 40 of Appl. 194 teaches wherein said anti-PVRIG antibody formulation comprises: i) a heavy chain comprising the heavy chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:8); and ii) a light chain comprising the light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13).
Regarding the instant claims 26 and 36, claim 41 of Appl. 245 teaches aid anti-PVRIG antibody formulation comprising:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain variable domain comprising the vhCDR1,vhCDR2, and vhCDR3 from the heavy chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:4), and ii) a light chain variable domain comprising the vlCDR1, vlCDR2, and vlCDR3 from the light chain variable domain of CHA.7.518.1.H4(S241P) (SEQ ID NO:9);(b) about 25 mM histidine; (c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and (e) about 0.01% % w/v polysorbate 80, wherein the composition has a pH from 6.5 +/- 0.2. Claim 37 of Appl. 194 teaches wherein said anti-PVRIG antibody is at a concentration of about 20 mg/mL.
Regarding the instant claims 27, claim 42 of Appl. 194 teaches said anti-PVRIG antibody formulation comprising:(a) an anti-PVRIG antibody, wherein said anti-PVRIG antibody comprises: i) a heavy chain comprising the heavy chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:8); and ii) a light chain comprising the light chain from CHA.7.518.1.H4(S241P) (SEQ ID NO:13);(b) about 25 mM histidine;(c) about 60 mM NaCl;(d) about 100 mM L-Arginine; and(e) about 0.01% % w/v polysorbate 80, wherein the composition has a pH from 6.5 +/- 0.2.
Regarding the instant claims 28-30, claims 43 and 46 of Appl. 194 teach wherein said anti-PVRIG antibody is administered at a dosage of about 0.01 mg/kg to about 20 mg/kg of the anti-PVRIG antibody or about 0.01 mg/kg to about 10 mg/kg of the anti- PVRIG antibody or about 10 mg/kg to about 20 mg/kg of the anti-PVRIG antibody; or about 0.01 mg/kg, 0.03 mg/kg, 0.1 mg/kg, 0.3 mg/kg, 1 mg/kg, 3 mg/kg, 10 mg/kg, or 20 mg/kg of the anti-PVRIG antibody (claim 43); wherein said anti-PVRIG antibody is administered 20 mg/kg every 4 weeks (claim 46).
Although the claims of Appl. 194 are drawn to a method, the claims disclose the pharmaceutical formulation as set forth above. One of ordinary skill in the art would have known to make the pharmaceutical formulation in order to perform the method of treatment of Appl. 194, thus reaches the instantly claimed invention.
Response to Arguments
For the rejection of claims 1-13, 16-23, 25-30, and 34-36 under Double Patenting applicant argues:
Applicant submits that the non-obviousness over White in view of Mhalasakant has been established by the arguments against the rejections under 35 U.S.C. § 103 provided above. The skilled artisan would not have been able to modify or combine White or Mhalasakant in order to arrive at the presently claimed stable liquid anti-PVIRG formulation with any reasonable
expectation of success.
Applicant is reiterating the arguments set forth above. Thus for the reasons set forth above the rejection is maintained.
NEW REJECTION
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 26 and 27 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 26, which depends on claim 1, does not recite “wherein the anti-PVRIG antibody is at a concentration of up to 40 mg/ml”. Thus, Given Broadest Reasonable Interpretation (BRI), the concentration of anti-PVRIG can be higher than 40 mg/ml. Thus, claim 26 fails to include all the limitations of the claim upon which it depends.
Claim 27, which depends on claim 1, does not recite “wherein the anti-PVRIG antibody is at a concentration of up to 40 mg/ml”. Thus, Given Broadest Reasonable Interpretation (BRI), the concentration of anti-PVRIG can be higher than 40 mg/ml. Thus, claim 26 fails to include all the limitations of the claim upon which it depends.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHENG LU whose telephone number is (571)272-0334. The examiner can normally be reached Monday-Friday 8-5.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis can be reached at (571)270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/CHENG LU/Examiner, Art Unit 1642
/SAMIRA J JEAN-LOUIS/Supervisory Patent Examiner, Art Unit 1642
Prosecution Insights