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 May 12, 2026 in response to the Office Action of January 13, 2026 is acknowledged and has been entered.
Claims 1, 2, 5, 6, 14, 15, and 17-20 have been amended.
Claims 3, 4, 11-13, and 16 have been cancelled.
Claims 21-30 have been added.
Claims 1, 2, 5-10, 14, 15, and 17-30 are pending.
Claims 20, 24 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions or species, there being no allowable generic or linking claim.
Claims 1, 2, 5-10, 14, 15, 17-19, 21-23, and 25-30 are currently under consideration as drawn to the elected invention.
It is noted that prior art does not teach/suggest an antibody or antigen-binding fragment specifically binds to a CCHFV protein Crimean Congo Hemorrhagic Fever Virus (CCHFV) protein comprising the elected CDRH1-3 and CDRL1-3 combination (the CDR combination of antibody: ADI-36121). The search has extended to other antibodies encompassed by claim 1 with written description support: 15 antibodies listed in Table 3: ADI-36120, ADI-36122, ADI-36125, ADI-36145, ADI-36193, ADI-37801, ADI-37817, ADI-37836, ADI-37842, ADI-37847, ADI-37849, ADI-42437, ADI-42462, ADI-42479, ADI-42623. Prior art does not teach/suggest these antibodies. However, these antibodies are natural occurring antibodies, thus new 101 rejection is made in this Office Action.
In view of amended Specification and new Sequence Listing filed May 12, 2026, the objection to Specification set forth in the Office Action of January 13, 2026 is hereby withdrawn.
In view of amended Drawing filed May 12, 2026, the objection to Drawing set forth in the Office Action of January 13, 2026 is hereby withdrawn.
In view of claim amendment filed May 12, 2026, the claim objection set forth in the Office Action of January 13, 2026 is hereby withdrawn.
In view of claim amendment filed May 12, 2026, the 112(b) rejection set forth in the Office Action of January 13, 2026 is hereby withdrawn.
In view of claim amendment filed May 12, 2026, the 112(a) rejection set forth in the Office Action of January 13, 2026 is hereby withdrawn, except for claim 14.
In view of claim amendment filed May 12, 2026, the Double Patenting rejection set forth in the Office Action of January 13, 2026 is modified.
MAINTAINED/MODIFIED REJECTIONS
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 14 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a WRITTEN DESCRIPTION rejection.
Claim 14 is drawn to an isolated human antibody and/or an antigen-binding fragment comprising CDRH1-3, CDRL1-2 and a CCHFV binding domain, CDRL3, wherein the CDRL3 encompasses a broad genus of variants. For example, the option a) alone encompasses 3456 (2x2x2x6x3x2x3x4) different CDRL3. The specification discloses Antibody Number 1 through Antibody Number 16 (Table 3), each of which has complete CDRH1-3 and CDRL1-3 structure. The specification does not disclose any antibody or antigen-binding fragment without complete CDRH1-3 and CDRL1-3 structure as set forth in the Antibody Number 1 through Antibody Number 16, or any antibody or antigen-binding fragment with CDR variants encompassed by the claim. Thus, the specification lacks written description support for the claimed antibodies or antigen-binding fragments that specifically binds to a CCHFV protein.
MPEP 2163 II A 3(a) states: Disclosure of an antigen fully characterized by its structure, formula, chemical name, physical properties, or deposit in a public depository does not, without more, provide an adequate written description of an antibody claimed by its binding affinity to that antigen, even when preparation of such an antibody is routine and conventional. See Amgen Inc. v. Sanofi, 872 F.3d 1367, 1378, 124 USPQ2d 1354, 1361 (Fed. Cir. 2017)("knowledge of the chemical structure of an antigen [does not give] the required kind of structure-identifying information about the corresponding antibodies"); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1351-52, 97 USPQ2d 1870, 1877 (Fed. Cir. 2011)(patent disclosed the antigen the claimed antibody was supposed to bind, but did not disclose any antibodies with the specific claimed properties).
By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three "complementarity determining regions" ("CDRs") which provide the majority of the contact residues for the binding of the antibody to its target epitope. Even a single point mutation in HCDR1 region could lead to antibody lose its binding activity (Ni et al., The Protein Journal, 43, pp. 683-696, July 2024, see Abstract, of record). Thus, one ordinary skill in the art would not be able to visualize other antibody encompassed by the claims, except Antibody Number 1 through Antibody Number 16, which binds to a CCHFV protein.
In the instant case, Table 3 of the specification describes 16 antibodies, each of which has complete CDRH1-3 and CDRL1-3 structure. The specification also discloses that the antibodies can bind to GnGc of CCHFV (Table 2, Fig. 5 and paragraph [0236] of the instant publication US 2023/0000979 A1). However, these antibodies would not tell the structure of other antibodies, variants or antigen-binding fragments thereof encompassed by the claim.
In addition, the claims identify the antibodies by function only, where the function is to: binds to a CCHFV protein. The specification has not established the relationship between the claimed functions and the structure of the antibody. One of ordinary skilled in the art would not be able to readily recognize/visualize an antibody or antigen-binding fragments thereof with required functions. Taken together, the specification has not provided sufficient evidence to show that the inventors possess a genus of antibodies or antigen-binding fragments as claimed.
Although Applicants may argue that it is possible to screen for antibodies with claimed properties/functions, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. "As we held in Lilly, "[a]n adequate written description of a DNA ... 'requires a precise definition, such as by structure, formula, chemical name, or physical properties,' not a mere wish or plan for obtaining the claimed chemical invention." 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171 ). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions." Knowledge of screening methods provides no information about the structure of any future antibodies or antibody fragments yet to be discovered that may function as claimed.
Taken together, the instant specification has not provided a sufficient description showing the necessary functional characteristics coupled with a known or disclosed correlation between functions and the structure. Thus, the specification is not sufficient to show the applicant was in possession of the genus of antibodies, variants, antibody fragments broadly encompassed claim 14.
Response to Arguments
For the 112(a) Written Description rejection, Applicant argues: the specification provide written description for the structural and functional features of the antibodies recited in amended claims 1, 14 and 15.
Applicant’s arguments have been fully considered but they are only partial persuasive. The 112(a) rejections for other claims are hereby withdrawn in view of claim amendments. However, the rejection for claim 14 is maintained. As set forth above, the amended claim 14 still encompasses a broad genus of CDRL3 variants. For example, the option a) alone encompasses 3456 (2x2x2x6x3x2x3x4) different CDRL3. The specification discloses Antibody Number 1 through Antibody Number 16 (Table 3), each of which has complete CDRH1-3 and CDRL1-3 structure. The specification does not disclose any antibody or antigen-binding fragment without complete CDRH1-3 and CDRL1-3 structure as set forth in the Antibody Number 1 through Antibody Number 16, or any antibody or antigen-binding fragment with CDR variants encompassed by the claim. In addition, the claims identify the antibodies by function only, where the function is to: binds to a CCHFV protein. The specification has not established the relationship between the claimed functions and the structure of the antibody. Thus, the specification is not sufficient to show the applicant was in possession of the genus of antibodies, variants, antibody fragments broadly encompassed by claim 14.
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.
Claims 1, 2, 5-10, and 14 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 of copending Application No. 17/308,753 (hereinafter Appl. 753).
It is noted that the instant application is a continuation-in-part of Appl. 753. Thus, the instant application share the same disclosure as Appl. 753, including antibodies and sequences in Table 3.
The claims of Appl. 753 teach:
1. An isolated human antibody or an antigen-binding fragment thereof that specifically binds to a Crimean Congo Hemorrhagic Fever Virus (CCHFV) protein, wherein at least one of the CDRH1, a CDRH2, a CDRH3, a CDRL1, a CDRL2, and CDRL3 amino acid sequence of the antibody or the antigen-binding fragment thereof is at least 70% identical to at least one the CDRH1, a CDRH2, a CDRH3, a CDRL1, a CDRL2, and/or a CDRL3 amino acid sequences disclosed in Table 3 of an antibody selected from Antibody Number 1 through Antibody Number 16 as disclosed in Table 3; and wherein said antibody or the antigen-binding fragment thereof also has one or more of the following characteristics: a) the antibody or antigen-binding fragment thereof cross-competes with said antibody or antigen-binding fragment thereof for binding to CCHFV; b) the antibody or antigen-binding fragment thereof displays a clean or low polyreactivity profile; c) the antibody or antigen-binding fragment thereof displays neutralization activity toward CCHFV in vitro; d) the antibody or antigen-binding fragment thereof displays an in vitro neutralization potency (IC50) of between about 0.5 microgram/milliliter (pg/ml) to about 5 pg/ml; or e) the antibody or antigen-binding fragment thereof binds to at least one of Gn, Gc, and a GnGc complex. Thus, claim 1 of Appl. 753 read on the amended claims 1 and 14.
2. The isolated antibody or antigen-binding fragment thereof of claim 1, wherein the antibody or antigen-binding fragment thereof comprises: at least two of characteristics a) through e). Thus, claim 2 of Appl. 753 read on the amended claim 2.
4. The isolated antibody or antigen-binding fragment thereof of claim 1, wherein the antibody or antigen-binding fragment thereof comprises: a) a heavy chain (HC) amino acid sequence of any one of the antibodies designated Antibody Number 1 through Antibody Number 16 as disclosed in Table 3; and b) a light chain (LC) amino acid sequence of any one of the antibodies designated Antibody Number 1 through Antibody Number 16 as disclosed in Table 3.
5. The isolated antibody or antigen-binding fragment thereof of claim 1, wherein the antibody is selected from the group consisting of antibodies that are at least 80% identical to any one of the antibodies designated as Antibody Number 1 through Antibody Number 16 as disclosed in Table 3. Thus, claim 5 of Appl. 753 reads on the amended claim 5.
6. The isolated antibody or antigen-binding fragment thereof of claim 4, wherein the antibody is selected from the group consisting of the antibodies designated as Antibody Number 1 through Antibody Number 16 as disclosed in Table 3. Thus, claim 6 of Appl. 753 reads on the amended claim 6.
7. An isolated nucleic acid sequence encoding an antibody or antigen- binding fragment thereof according to claim 1. Thus, claim 7 of Appl. 753 reads on the instant claim 7.
8. An expression vector comprising the isolated nucleic acid sequence according to claim 7. Thus, claim 8 of Appl. 753 reads on the instant claim 8.
9. A host cell transfected with the expression vector according to claim 8. Thus, claim 9 of Appl. 753 reads on the instant claim 9.
10. A pharmaceutical composition comprising: one or more of the isolated antibodies or antigen-binding fragments thereof according to claim 1 and a pharmaceutically acceptable carrier and/or excipient. Thus, claim 10 of Appl. 753 reads on the instant claim 10.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 15, 17-19, 21-23, and 25-30 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-14 of copending Application No. 17/308,753 (hereinafter Appl. 753), as applied to claims 1-10 and 14 above, in view of Asokan (Asokan et al., Journal of Virology, Volume 89, Number 24, 12501-12512, Publication Date: 10/7/2015, of record) and Brinkmann (Brinkmann et al., MABS, 2017, VOL. 9, NO. 2, 182-212, Publication Date: 01/10/2017, of record)
The claims of Appl. 753 teach Antibody Number 1 through Antibody Number 16 of Table 3 which reads the antibodies of instant claim 1, as set forth above. However, the claims of Appl. 753 do not teach dual-variable domain antibodies in a format as defined by claims 15, 17-19, 21-23, or isolated nucleic acid, expression vector, host cells or pharmaceutical compositions of claims 25-30.
Asokan teaches the physical combination of two neutralizing antibodies may improve coverage and neutralization potency over the individual parental antibodies (Abstract). Asokan teaches that the ability of bispecific IgGs to recognize either of two neutralization epitopes led to improved neutralization coverage and may have advantages with regard to preventing neutralization escape (page 12510, col. 2, para. 2).
Brinkmann teaches various ways to make bispecific antibody, for example DVD-Ig format (Fig. 2, box 12), in which the first heavy chain variable domain is liner to a second heavy chain variable domain through a linker and the first light chain variable domain is liner to a second light chain variable domain through a linker.
Brinkmann teaches that dual-variable-domain antibody (DVD-Ig) format have been widely used in the field (page 197, col. 2, para. 2).
Brinkmann teaches that the linkers connecting two variable domains within one chain, usually 5 to 13 residues, such as G4S (page 197, col. 2, para. 2).
Brinkmann teaches that in DVD-Ig format, the outer binding site is highly mobile and can fold out of the plane to allow binding of the inner binding site (page 197, col. 2, para. 2).
It would have prima facie been obvious to one of ordinarily skilled in the art before the invention was filed to modify the antibody taught by the claims of Appl. 753, such as ADI-36121 (SEQ ID NO: 35 + SEQ ID NO: 36) and ADI-37801 (SEQ ID NO: 45 + SEQ ID NO: 46), and to make a bispecific antibody by physically linking the antibodies with linkers such as G4S, because Asokan teaches bispecific IgGs to recognize either of two neutralization epitopes led to improved neutralization coverage and may have advantages with regard to preventing neutralization escape, and to use the DVD-Ig format to make the bispecific antibodies, because Brinkmann teaches that the DVD-Ig format with linkers have been widely used in the field and maintain binding activity for both antigen-binding domains. Based on the teachings of the claims of Appl. 753 , Asokan and Brinkmann, one of ordinary skill in the art would have had a reasonable expectation that the combination of ADI-36121 (SEQ ID NO: 35 + SEQ ID NO: 36) and ADI-37801 (SEQ ID NO: 45 + SEQ ID NO: 46) in a DVD-Ig format would generate a dual-variable domain antibody with improved neutralization coverage and have advantages with regard to preventing neutralization escape. The motivation would have been to develop a more potent antibody for neutralizing CCHFV.
Regarding claims 26-30, as set forth above, claims of App. 753 teaches isolated nucleic acid sequence encoding an antibody; an expression vector comprising the isolated nucleic acid; a host cell comprising the expression vector; a pharmaceutical composition comprising the antibody and a pharmaceutically acceptable carrier and/or excipient. It would have prima facie been obvious to one of ordinarily skilled in the art before the invention was filed to make the products of instant claims 26-30 for making and using the antibody of instant claim 15.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
For the Double Patenting rejection, Applicant argues:
Applicant respectfully requests that the Examiner hold the rejection in abeyance until the claims of this application and the copending '753 application are found otherwise allowable.
Applicant’s arguments have been fully considered but they are not persuasive because the claims of the instant application are still anticipated or obvious in view of the co-pending claims and a terminal disclaimer has not been filed. Thus, the rejections above are maintained for the reasons of record.
NEW REJECTIONS
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 2, 5-7, 10 and 14 are rejected under 35 U.S.C. 101 because the claimed invention is directed to naturally occurring products/phenomenon without significantly more. The claims recite an isolated human antibody or an antigen-binding fragment thereof that specifically binds to a Crimean Congo Hemorrhagic Fever Virus (CCHFV) protein, comprising any CDRH1-3 and CDRL1-3 combination of a) to p). The recited CDR combinations corresponding to the antibodies of Table 3. As evidenced by paragraph [0209] of the instant specification US 2023/0000979 A1, these antibodies isolated from human. Example 1 indicates that the antibodies are isolated from four CCHFV-convalescent adult donors. Thus, claim 1 encompasses natural occurring antibodies (natural product). This judicial exception is not integrated into a practical application as explained below. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception.
As explained in MPEP 2106.04(11) and the October 2019 Update, a claim “recites” a judicial exception when the judicial exception is “set forth” or “described” in the claim. The eligibility analysis comprises three-step tests: 1) Step 2A Prong one: evaluating whether the claim recites a judicial exception (MPEP 2106.3); 2) Step 2A Prong two: evaluating whether the claim as a whole integrates the recited judicial exception into a practical application of the exception (MPEP 2106.4); 3) Step 2B: evaluating whether the claim as a whole amounts to significantly more than the recited exception (MPEP 2106.5).
As set forth above, the present claims are directed to a product so Step 1 is satisfied.
For Prong One of Step 2A claim 1 recites a judicial exception, i.e. n isolated human antibody or an antigen-binding fragment thereof that specifically binds to a Crimean Congo Hemorrhagic Fever Virus (CCHFV) protein, comprising any CDRH1-3 and CDRL1-3 combination of a) to p). As set forth above, the antibodies in Table 3 are isolated from four CCHFV-convalescent adult donors. Thus, claim 1 encompass naturally occurring antibodies. So the answer to Prong One of Step 2A is yes, the claims do recite a judicial exception: natural product.
Claim 1 recites a judicial exception, as set forth above, and the analysis must therefore proceed to Step 2A Prong Two.
Step 2A Prong Two: This part of the eligibility analysis evaluates whether the claim as a whole integrates the recited judicial exception into a practical application of the exception. This evaluation is performed by (a) identifying whether there are any additional elements recited in the claim beyond the judicial exception, and (b) evaluating those additional elements individually and in combination to determine whether the claim as a whole integrates the exception into a practical application. 2019 PEG Section III(A)(2), 84 Fed. Reg. at 54-55.
Claim 1 recites the additional element of “an isolated …”. However, because the antibody’s structure and function are identical to what exists in the body, merely removing it from its natural environment does not make the antibodies markedly different. Claim 1 therefore recites simply naturally occurring antibodies without additional elements of the claim which would integrate the judicial exception into a practical application (Step 2A: YES).
Step 2B: This part of the eligibility analysis evaluates whether the claim as a whole amount to significantly more than the recited exception, i.e., whether any additional element, or combination of additional elements, adds an inventive concept to the claim. Regarding Step 2B, claim 1 does not recite any additional elements which amount to significantly more than the judicial exception recited. There are no markedly distinct characteristics of an isolated antibody required by claim 1 which confer structural elements distinct from natural antibodies. Therefore, claim 1 is not eligible subject matter under 35 USC 101.
Regarding claim 2, the recited functions are the functions possessed by the natural antibodies (e.g. antibody 1 to antibody 16 of Table 3), as evidenced by [0240] of the instant publication US 2023/0000979 A1. Claim 2 therefore recites simply natural function associated with the natural antibody without additional elements which would integrate the judicial exception into a practical application. Claim 2 is therefore not eligible subject matter.
Regarding claims 5 and 6, as evidenced by Table 3, the recited VH and VL sequences are the VH and VL of natural antibodies. Thes claims are therefore not eligible subject matter.
Claim 7 recites an isolated nucleic acid sequence encoding an antibody or anti-gen binding fragment of claim 1. Thus, the claim encompasses natural nucleic acid sequences encoding natural antibodies (e.g. antibody 1 to antibody 16 of Table 3). As set forth above, because the nucleic acid sequence’s structure and function are identical to what exists in the body, merely removing it from its natural environment does not make the isolated nucleic acid sequence markedly different. Claim 7 is therefore not eligible subject matter.
Claim 10 recites a pharmaceutical composition comprising a natural antibody and a pharmaceutically acceptable carrier and/or excipient. However, mixing a natural antibody with a basic carrier (like saline or water) does not change the nature of the antibody itself. In addition, Simply putting a natural antibody in a buffer does not add enough innovative, man-made features to make the composition eligible for a patent.
Claim 14 recites degenerate CTR sequences and encompasses CTRs of natural antibodies (e.g. antibody 1 to antibody 16 of Table 3), without additional elements. Claim 14 is therefore not eligible subject matter.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 22 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 22 recites “wherein the first heavy and light chain variable domains and the second heavy and light chain variable domains comprise: a) SEQ ID NO: 35 and SEQ ID NO: 36; b) SEQ ID NO: 45 and SEQ ID NO: 46; or c) SEQ ID NO: 41 and SEQ ID NO: 42” which is ambiguous. The antibody has two heavy chain variable domains and two light heavy chain variable domains, however, the options a) to c) only provide SEQ ID NOs for one heavy chain variable domain and one light chain variable domain. It is unclear how the two recited sequences are applied to the four variable domains.
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.
Claim 5 is 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 5, which depend on claim 1, recites a VH amino acid sequence with at least 80% sequence identity with SEQ ID NO: XXX and a VL amino acid sequence with at least 80% sequence identity with SEQ ID NO: XXX. Claim 1 recites antibodies with specific CDRH 1-3 and CDRL1-3 combinations. If an antibody only require 80% identity for the VH and VL sequence, the antibody could have variations in the CDR regions. This would violate the independent claim’s requirement that the 6 specific CDRs must be present. In addition, claim 5 recites “d) a VH amino acid sequence with at least 80% sequence identity with SEQ ID NO: 39 and a VL amino acid sequence with at least 80% sequence identity with SEQ ID NO: 40”. As indicated in Table 13 on page 67, light chain variable region of ADI-36125 comprises the sequence of SEQ ID NO: 40. However, SEQ ID NO: 40 only have two CDRs corresponding to SEQ ID NO:93 and SEQ ID NO: 94, respectively. SEQ ID NO: 40 does not comprise CDRL3 of SEQ ID NO: 20, which is required by claim 1 d). Taken together, claim 5 fails to include all the limitations and broadens the scope of the claim upon which it depends.
Claim 6 is 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 6, which depend on claim 1, recites “d) a VH amino acid sequence of SEQ ID NO: 39 and a VL amino acid sequence of SEQ ID NO: 40”. As indicated in Table 13 on page 67, light chain variable region of ADI-36125 comprises the sequence of SEQ ID NO: 40. However, SEQ ID NO: 40 only have two CDRs corresponding to SEQ ID NO:93 and SEQ ID NO: 94, respectively. SEQ ID NO: 40 does not comprise CDRL3 of SEQ ID NO: 20, which is required by claim 1 d). Taken together, claim 6 fails to include all the limitations and broadens the scope of the claim upon which it depends.
Claim 17 is 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 17, which depend on claim 15, recites a VH amino acid sequence with at least 80% sequence identity with SEQ ID NO: XXX and a VL amino acid sequence with at least 80% sequence identity with SEQ ID NO: XXX. Claim 15 recites antibodies with specific CDRH 1-3 and CDRL1-3 combinations. If an antibody only require 80% identity for the VH and VL sequence, the antibody could have variations in the CDR regions. This would violate the independent claim’s requirement that the 6 specific CDRs must be present. In addition, claim 17 recites in i)d) and ii)d): “a VH amino acid sequence with at least 80% sequence identity with SEQ ID NO: 39 and a VL amino acid sequence with at least 80% sequence identity with SEQ ID NO: 40”. As indicated in Table 13 on page 67, light chain variable region of ADI-36125 comprises the sequence of SEQ ID NO: 40. However, SEQ ID NO: 40 only have two CDRs corresponding to SEQ ID NO:93 and SEQ ID NO: 94, respectively. SEQ ID NO: 40 does not comprise CDRL3 of SEQ ID NO: 20, which is required by claim 15 d). Taken together, claim 17 fails to include all the limitations and broadens the scope of the claim upon which it depends.
Claim 21 is 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 21, which in directly depend on claim 15, recites in i)d) and ii)d): “a VH amino acid sequence of SEQ ID NO: 39 and a VL amino acid sequence of SEQ ID NO: 40”. As indicated in Table 13 on page 67, light chain variable region of ADI-36125 comprises the sequence of SEQ ID NO: 40. However, SEQ ID NO: 40 only have two CDRs corresponding to SEQ ID NO:93 and SEQ ID NO: 94, respectively. SEQ ID NO: 40 does not comprise CDRL3 of SEQ ID NO: 20, which is required by claim 15 d). Taken together, claim 21 fails to include all the limitations and broadens the scope of the claim upon which it depends.
Applicant may cancel the claims, amend the claims to place the claims in proper dependent form, rewrite the claims in independent form, or present a sufficient showing that the dependent claims complies with the statutory requirements.
Conclusion
No claims are allowed.
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/CHENG LU/ Examiner, Art Unit 1642
/SAMIRA J JEAN-LOUIS/Supervisory Patent Examiner, Art Unit 1642
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