Detailed Action
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 .
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 7 November 2025 (referred to herein as remarks) has been entered.
Status of the Claims
Claims 1-13 were originally filed 6 December 2024. Claims 14-17 were added in response
to non-final received 11 June 2025. Claims 1-7, 10-15, and 17 are currently pending
and under consideration.
Withdrawn Rejections
In view of Applicant’s amendments all previous art rejections are hereby withdrawn.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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, 2, 10-13, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over WO2022183502 A1 (referred to herein as Du, as cited on the PTO-892 dated 03/12/2025) published 9 September 2022, US Patent Publication 2023/0099149 (referred to herein as Kraiem, as cited on the PTO-892 dated 03/12/2025) published 30 March 2023, and Beerli (see Beerli et al. (2015). Sortase Enzyme-Mediated Generation of Site-Specifically Conjugated Antibody Drug Conjugates with High In Vitro and In Vivo Potency. PLoS ONE 10(7): e0131177). It is noted US Patent Publication 2024/0150455 A1 will be used as an English translation given Du and US Patent Publication 2024/0150455 A1 have the same underlying PCT and therefore the same disclosure.
Du discloses an anti-CDLN6 antibody with identical HCDRs, LCDRs, VH, VL, and LC to the instantly claimed antibody drug conjugate (see Du pg. 4, para [0074, 0079, and 0084], pg. 7 para [0182], claim 35(3)). The CLDN-6 antibody or antigen binding domain can be linked to a therapeutic agent (see Du pg. 8 para [0201]). In particular, the therapeutic agent is a topoisomerase inhibitor such as a camptothecin derivative (e.g., irinotecan, topotecan, etc.) (see Du para spanning pgs. 8-9, para [0210], claim 42(2)). The cytotoxic agent can be conjugated via a linker such as a peptide or pH sensitive linker (e.g., cathepsins) (see Du pg. 9 para [0214, 0215]). Additionally, Du claims a method of treating a tumor comprising administering to a subject in need thereof an effective amount of an immunoconjugate comprising the CLDN6 antigen binding domain wherein the tumor is selected from ovarian, lung, gastric, ear nose throat (ENT), endometrial, liver cancer (see specification pg. 8 para [0201], claim 51(3), optionally (2)). Du teaches the an identical anti-CDLN6 antigen binding domain conjugated to a camptothecin derivative via a cathepsin linker.
Kraiem teaches a Nectin-4 antigen binding domains conjugated to a camptothecin analogue or derivative, such as exatecan or SN-38 for use in the treatment of cancers (see Kraiem abstract, pg. 2 para [0010], [0020]).The highly potent linkers can be conjugated to an antibody that binds a tumor antigen (see Kraiem pg. 2 para [0011]). In particular embodiments, Kraiem also specifies the antibody drug conjugate has the following components in the following order:
Nectin-4 antigen binding domain,
a protected reactive group capable of reacting with a complementary reactive group on an antigen binding protein,
a spacer moiety (Y),
a di-peptide-cleavable moiety (e.g., valine-citrulline, valine alanine, or phenylalanine-lysine),
a self-eliminating spacer system (Yʹ), and lastly
a camptothecin analogue such as exatecan or SN-38 (see Kraiem pgs. 4-5 para [0044]).
Kraiem teaches a linker can function as a spacer or stretcher to distance an antibody from Z (i.e., the drug) in order to avoid interference with the antigen binding function. In addition, Y can be a molecule that forms a bond with an amino acid of the antibody (e.g., sulfur atom) and which spacer or stretcher (Y) links the antibody to a cleavable amino acid unit (see Kraiem pg. 21 para [0228]). The spacer chain Y can generally be any single molecular weight homopolymer with 1-6 units of the monomer (see Kraiem pg. 22 para [0232]). Specifically, Kraiem discloses the following exemplary structure (see Kraiem pg. 32, first structure):
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The maleimide group is conjugated to the antigen binding domain via cysteine residues (see Kraiem pg. 30 para [0300]). In addition, the Yʹ group is p-aminobenzylcarbamate in particular embodiments (see Kraiem para [0240] spanning pgs. 22-23). The antibody drug ratio is an integer from 4-8 (see Kraiem para [0062]). Kraiem also teaches each of the exatecan linkers when conjugated to the Nectin-4 antibody permitted efficient killing of the Nectin-4 low expressing SUM190 cells (see Kraiem pg. 48 para [0412], figure 7, see structures on pgs. 47 and 48).
Beeril discloses ADCs comprising glycine spacers with VC-PAB-cytotoxic payloads are both functional and potent (see Beeril pg. 7, figure 2B, pg. 8, 3rd para). Specifically, IC50 values for Adcetris=10.2ng/ml ±4.3ng/ml while the cAc10-Gly5-VC-PAB-MMAE=11.8ng/ml ±2.4ng/ml (see Beeril pg. 9). In addition, Beeril discloses the ADC function was mediated by binding specificity (see Beeril pg. 10, 1st para). It is noted the Gly5 spacer was functional in the context of the Her-2 antigen binding domain, trastuzumab, and different cytotoxic payloads (e.g., DM1 and maytansinoid).
Therefore a person of ordinary skill in the art would conjugate the maleimide-PEG-Val-Ala-PAB-Exatecan taught by Kraiem to the CLDN6 antigen binding domain taught by Du given Du teaches the antigen binding domain as an ADC comprising a topoisomerase inhibitor and Kraiem teaches a functional linker drug combination comprising a topoisomerase inhibitor. In addition, the ordinary artisan would substitute the PEG spacer taught by Kraiem for a polyglycine spacer as taught by Beeril as these are art recognized equivalents for the same purpose. Kraiem discloses the spacer functions to create distance between the cytotoxic payload and the antigen binding domain. Beeril discloses polyglycine functions as a suitable spacer in ADCs comprising Val-Cit-PAB-cytotoxic payloads; thereby providing a reasonable expectation of success.
Applicant's arguments filed 7 November 2025 (referred to herein as Remarks) have been fully considered but they are not persuasive.
Applicant argues unexpected results regarding aggregation. Specifically, the trend in reduced aggregation could be extrapolated to polyglycine linkers longer than 5 residues (see Remarks para spanning pgs. 16-17) and the claims are commensurate in scope with unexpected results (see Remarks pg. 18, 1st para).
First, it was known in the art that polyglycine chains longer than 5 residues are normally insoluble in water (see Bykov and Asher (2010) Raman studies of solution polyglycine conformations. J. Phys. Chem. B. Vol 114, Iss. 19, pgs. 6636-6641, in particular pg. 6636, 1st col. 3rd para). Thus, the ordinary artisan would not expect the reduced aggregation seen with 5 glycine’s compared to 3 glycine’s to be indicative of reduced aggregation with 8 glycine’s. Second, Applicant’s aggregation results are drawn to an ADC comprising Seq ID No: 22 (i.e., 3 glycine spacer) or Seq ID No: 21 (i.e., 5 glycine spacer) using cite specific conjugation (i.e., a particular DAR) linked to Val-Ala-PABC-exatecan (see specification 35 last para, pg. 36, last para). The claims are drawn to a genus of structures comprising an antigen binding domain with particular CDRs comprising any framework, heavy and light chain regions, any DAR of 1-6, glycine spacer of 5-8, and a val-ala or val-cit, any self immolative moiety, linked to any cysteine residue on the antibody (see claim 1). Therefore, the claims remain drawn to a genus of structures wherein the unexpected result of reduced aggregation is affected by any number of variables the instant claims recite as genera, such as, the DAR, glycine linker size, conjugation site, and the overall structure (e.g., an antigen binding domain vs a full length antibody). Thus, as previous stated the claims are not commensurate in scope with Applicant’s allegedly unexpected results (see Final mailed 07/07/2025 pg. 10 last full sentence). In addition, Beeril demonstrates ADCs comprising Gly5-VC-PAB-MMAE with a DAR of approximately 3.18 had 95.8% monomers while the 5 glycine spacer with alternative antigen binding domains and cytotoxic payloads had even better yields (see Beeril pg. 8 Table 1). Therefore, the Applicant’s aggregation results with a 5 glycine spacer are entirely expected.
Claims 1, 2, 4, 5, 10-14, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Du, Kraiem, Beeril and Cho (as cited on the PTO-892 mailed 07/07/2025). It is noted US Patent Publication 2024/0150455 A1 will be used as an English translation given Du and US Patent Publication 2024/0150455 A1 have the same underlying PCT and therefore the same disclosure.
The teachings of Du, Kraiem, and Beeril are set forth above.
Cho teaches method of site specific conjugation of a maleimide-PEG spacer-cathepsin cleavage site-SG3199 to cysteine 220 on the heavy chain of a PSMA antibody (see Cho pg. 2177, 1st col. 2nd para, pg. 2182, 2nd col. last para). The site specific conjugation uses cysteine to valine substitutions in the HC at positions 226 and 229 and a cysteine to serine substitution in the LC at position 214 (see Cho pg. 2177 1st col. 4th para). The substitutions at these particular positions facilitated the site specific conjugation at position 220 (see Cho. pg. 2177 1st col. 4th para). The resulting ADC has a safety profile consistent with a previously studied ADC comprising the same linker drug (see Cho pg. 2184, 1st col. 3rd para).
A person of ordinary skill in the art would further modify the CLDN6 antigen binding domain conjugated to a Mal-Gly5-Val-Ala-PAB-exacetan as made obvious by Du, Kraiem, and Beeril by substituting up to three cysteines in the antibody hinge region as taught by Cho in order to facilitate the site specific conjugation of the linker payload taught by Kraiem and modified by Beeril to the antibody taught by Du. This is pertinent to instant claims 4 and 5.
Claims 1, 2, 4-6, 10-15, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Du, Kraiem, Beeril, Cho, and Dimasi (as cited on the PTO-892 mailed 03/12/2025). It is noted US Patent Publication 2024/0150455 A1 will be used as an English translation given Du and US Patent Publication 2024/0150455 A1 have the same underlying PCT and therefore the same disclosure.
The teachings of Du, Kraiem, Beeril and Cho are set forth above.
Dimasi teaches the three most common sites in the Fc region used for conjugation of linker drug ADC are A114 in the CH1 domain, S239 in the CH2 domain, and V205 in the CL kappa domain (see Dimasi pg. 1502, 1st col. 3rd para, pg. 1505 figure 2). These particular sites do no impact expression, purification yields, or thermal stability, and do no destabilize the structure (see Dimasi pg. 1502, 1st col. 3rd para, pg. 1513, 2nd col. 2nd para). Furthermore, the cysteine substitutions results in sulfhydryls with high reactivity toward maleimides bearing cytotoxic payloads (see Dimasi pg. 1502, 1st col. 3rd para). Dimasi also teaches the Fc-mediated mechanisms of action are not desirable in particular therapeutic settings, such as ADCs, and it may be beneficial to have a silent Fc with no or reduced binding to FcγRs (see Dimasi pg. 1513, 2nd col. last para).
Therefore, a person of ordinary skill in the art would further substitute a valine to cystine at position 205 of the kappa light chain as taught by Dimasi in the CLDN-6 antibody conjugated to exatecan as taught by Du to a specific cysteine in the antibody hinge region as taught by Cho, using the linker drug payload taught by Kraiem and modified by Beeril in order to engineer a second site specific position for conjugation of the antibody drug linker.
Claims 1, 2, 4-7, 10-15, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Du, Kraiem, Jackson, Cho, Dimasi, and Pejchal (as cited on the PTO-892 mailed 03/12/2025). It is noted US Patent Publication 2024/0150455 A1 will be used as an English translation given Du and US Patent Publication 2024/0150455 A1 have the same underlying PCT and therefore the same disclosure.
The teachings of Du, Kraiem, Beeril, Cho, and Dimasi are set forth above.
Pejchal teaches particular mutations sets that are effective for eliminating Fc effector functions with the retention of wildtype-like stability (see Pejchal abstract). Pejchal teaches that combining either an S267K, P329G, and P329A with lower hinge mutations LALA and LALE completely eliminates FcγR binding while retaining wildtype like biophysical properties (see Pejchal pg. 2 last para, pg. 9, 1st para, figure 3B). Specifically the LALA-P329A mutations performed very similarly to the LALA-P329G in terms of abolishing effector function while retaining stability and biophysical developability profile (see Pejchal pg. 11, last para). In addition, regarding the mutational sets Pejchal teaches, “it is unlikely that the functional properties of the newly generated mutations sets would fall outside of expectations based on these historical assessments” (see Pejchal pg. 12 last para).
Therefore, a person of ordinary skill in the art would engineer the CLDN-6 antibody in an immunoconjugate taught by Du to comprise the L234A, L235A, and P329A substitutions as taught by Pejchal given Pejchal teaches these mutations silent the FcγR and C1q functions even under more sensitive assay conditions while maintaining stability and biodevelopability. In addition, Dimasi also teaches ADCs may benefit from silent Fc regions in order to maintain antibody half-life while eliminating the undesirable effector functions.
Claims 1, 2, 3, and 10-13 are rejected under 35 U.S.C. 103 as being unpatentable over Du, Kraiem, Jackson, and Stapleton (as cited on the PTO-892 mailed 03/12/2025). It is noted US Patent Publication 2024/0150455 A1 will be used as an English translation given Du and US Patent Publication 2024/0150455 A1 have the same underlying PCT and therefore the same disclosure.
The teachings of Du, Kraiem, and Beeril are set forth above.
It is noted Du discloses a HC with 99.4% sequence identity wherein the heavy chain differs from the instantly claimed heavy chain at position 355 and 357 (see Du pg. 7 para [0180]; see sequence comparison below).
Stapleton teaches an IgG1 Fc region wherein 2 allotypic residues in CH3 are substituted, i.e., D356E, L358M) and said substitutions do not affect the properties of the constant region (see Stapleton pg. 2, 1st col. 1st para). These substitutions were made to correspond to the IgG2 residues (see Stapleton pg. 2, 1st col. 1st para, figure 1).
Therefore, a person of ordinary skill in the art would have substituted the E356 and M358 taught by Du for aspartate and leucine, respectively, given these are the residues in the naturally occurring IgG1 Fc region and these Fc regions are both art recognized equivalents/variations of each other. This is pertinent to instant claim 3.
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 1-7, 10-15, and 17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 4, 6, 8, and 9 of U.S. Patent No. 18/969,940 (referred to herein as ‘940 application) in view of Du, Cho, Dimasi, Pejchal, and Stapleton.
The ‘940 application claims an antibody drug conjugate comprising an identical linker drug conjugate formula wherein the linker (i.e., L) is a species of the instantly claimed L. Pursuant to MPEP § 2131.02 a generic claim cannot be allowed to an applicant if the prior art discloses a species falling within the claimed genus. In re Slayter, 276 F.2d 408, 411, 125 USPQ 345, 347 (CCPA 1960); In re Gosteli, 872 F.2d 1008, 10 USPQ2d 1614 (Fed. Cir. 1989). Subsequent dependent claims recite identical linker drug structure (see ‘940 claim 6), cathepsin cleavable sequence (see ‘940 claim 3), self-immolative moiety (see ‘940 claim 4), and antibody drug ration (see ‘940 claim 8) as set forth in instant claims 1 and 8-12. The ‘940 application does not claim a CLDN6 antigen binding domain, conjugation to a cysteine in the hinge region and at LC position 205, a silent Fc region, or the method of treating a proliferative disease.
The teachings of Du, Cho, Dimasi, Pejchal, and Stapleton.
Therefore, a person of ordinary skill in the art would substitute the PSMA antibody recited in the ‘940 application for the CLDN6 antigen binding domain and subsequent full length antibody taught by Du and Stapleton. This is pertinent to instant claims 1-3 and 8-12. In addition, a person of ordinary skill in the art would substitute treating a proliferative disease characterized by overexpression of PSMA as claimed by the ‘940 application for a proliferative disease such as ovarian cancer as taught by Du. This is pertinent to instant claim 13.
Regarding claims 4 and 5, a person of ordinary skill in the art would substitute up to three cysteines, including cysteine 226, in the antibody hinge region set forth by Du and Stapleton and as taught by Cho in order to facilitate site specific conjugation of the linker drug claimed by the ‘940 application.
Regarding claim 6, a person of ordinary skill in the art would further modify the antibody drug conjugate to include a second site specific conjugation site as taught by Dimasi.
Regarding claim 7, a person of ordinary skill in the art would further modify the antibody drug conjugate to comprise a L234A, L235A, and P329A substitution in the Fc region in order to silence the antibody effector functions as taught by Dimasi and Pejchal given Dimasi teaches antibody drug conjugates may benefit from reduce effector functions.
This is a provisional nonstatutory double patenting rejection.
Applicant's arguments filed 7 November 2025 (referred to herein as Remarks) have been fully considered but they are not persuasive.
Applicant argues the ‘940 application has no teaching motivation or suggestion to modify the claimed anti PSMA ADC to an anti-Claudin-6 ADC (see Remarks pg. 18, last para) and the unexpected results discussed above (see Remarks para spanning pgs. 18-19).
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). Du teaches the instantly claimed anti-claudin-6 antigen binding domain in the form of an ADC linked to a topoisomerase inhibitor while the ‘940 application teaches a functional topoisomerase inhibitor linker drug combination. See above for a response regarding the allegedly unexpected results.
Therefore the provisional non-statutory double patenting rejection of claims 1-7, 10-13, and 17 is hereby maintained.
Sequence Comparison
(Qy) Instant Seq ID No: 1 compared to (Db) Du Seq ID No: 19
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(Qy) Instant Seq ID No: 2 compared to (Db) Du Seq ID No: 20
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321
633
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(Qy) Instant Seq ID No: 11 compared to (Db) Du Seq ID No: 22
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320
639
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(Qy) Instant Seq ID No: 11 compared to (Db) Du Seq ID No: 22
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314
655
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(Qy) Instant Seq ID No: 9 compared to (Db) Du Seq ID No: 19
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320
632
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(Qy) Instant Seq ID No: 9 compared to (Db) Du Seq ID No: 21
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534
637
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Conclusion
No claim allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to HILARY ANN PETRASH whose telephone number is (703)756-4630. The examiner can normally be reached Monday-Friday 8:30-4:30 EST.
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/H.A.P./Examiner, Art Unit 1644 /AMY E JUEDES/Primary Examiner, Art Unit 1644
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