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 .
The response filed 1-22-2026 has been entered into the record. Claims 1-19 are pending.
Sequence Compliance
Sequence Requirements
This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 C.F.R. § 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 C.F.R. § § 1.821-1.825 for the reason(s) set forth below. The drawings recite sequences that are not followed by a specific sequence identifier either in the dawning per se or in the Brief Description of the Figures/
Drawings in the specification. Correction is required. Full compliance with the sequence rules is required in response to this office action.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
It is noted that the priority date for the claims is the antibody-drug conjugates (ADCs) comprising a nectin-4 antibody and an amatoxin are only disclosed in the priority application EP21209332.2 filed 11/19/2021. The other earlier priority EP applications only disclose conjugation of specific antibodies to alpha-amanitin and specific disclosed antibodies enfortumab, ch15.A7.5 and ch-9A2.7 to generate ADCs. As such, the claims are only entitled to the filing date of 11/19/2021.
Election/Restrictions
Applicant’s election of Group I, species
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in the reply filed on 1-22-2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Claims 9 and 10 are withdrawn from consideration as not providing an explicit embodiment that covers the elected invention. Claims 17-19 are withdrawn from consideration as not reading on the elected invention.
Information Disclosure Statement
The information disclosure statement has been considered. An initialed copy is enclosed.
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 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.
Claims 1-8 and 11-16 are rejected under 35 U.S.C. 112(a), 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
The claims are drawn to antibody drug conjugates where the antibody binds Nectin-4 and the drug is an amatoxin. The claims encompass antibodies, polyclonal, monoclonal, chimeric, humanized, single chain (VH or VL being optional etc) bispecific that bind a Nectin-4 antigen, chimeric antibodies, binding fragments of chimeric antibodies and percent variations, substitutions, insertions of CDRs and combinations of different VH and VL that do not include all 6 conventional complementary determining regions (CDRs) of the starting monoclonal antibodies. The claims encompass random combinations of different variable heavy and variable light chain regions or single chain antibodies having only a VH or VL. The claims encompass unlimited variation of the elected CDRs alone or in combination with others. The variation within the genus is enormous. In AbbVie Deutschland GmbH & Co. v. Janssen Biotech, Inc., Ill USPQ2d 1780 (Fed. Cir. 2014) AbbVie had claims to functionally claimed antibodies and Centocor presented evidence that the antibodies described in AbbVie's patents were not representative of other members of the functionally claimed genus. The decision states, “When a patent claims a genus using functional language to define a desired result, ‘the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.’ Id. at 1349. We have held that 'a sufficient description of a genus ... requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can “visualize or recognize” the members of the genus.’ Id. at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). Here, the claimed invention is a class of fully human antibodies that are defined by their high affinity and neutralizing activity to human IL-12, a known antigen. AbbVie's expert conceded that the '128 and '485 patents do not disclose structural features common to the members of the claimed genus.” The AbbVie decision considers how large of a genus is involved and what species of the genus are described in the patent. With the written description of a genus, however, merely drawing a fence around a perceived genus is not a description of the genus. One needs to show that one has truly invented the genus, i.e., that one has conceived and described sufficient representative species encompassing the breadth of the genus. Otherwise, one has only a research plan, leaving it to others to explore the unknown contours of the claimed genus. See Ariad, 598 F.3d at 1353 (The written description requirement guards against claims that “merely recite a description of the problem to be solved while claiming all solutions to it and ... cover any compound later actually invented and determined to fall within the claim's functional boundaries.”).
The specification discloses a four monoclonal antibodies having particular binding properties to the nectin-4 cancer antigen and particular combination of CDRs. The specification does not teach which residues of the monoclonal antibodies of the specification can be varied and still perform the requisite function. It is well established that changes in the amino acid sequence of the variable region of an antibody create new antibodies with highly unpredictable binding characteristics. See for example Kussie et al (1994, Table I) which teaches that substitution of a single amino acid can totally ablate antigen binding. As a further demonstration of the unpredictability of substitute or mutated antibodies, see Chen et al, (1995). The reference again teaches that the substitution of a single amino acid can totally ablate antigen binding (Figure 1), however, the reference additionally teaches that the same substitution in closely related antibodies can have opposite effects. The authors compared the effects of identical substitution in related antibodies D16 and T15, and as shown in Figure 3, some substitutions increased antigen binding in one antibody while ablating it in the other.
The state of the art recognized that in general all three CDRs of the heavy chain variable region AND all three CDRs of the light chain variable region were important for determining the ability of an antibody in any of a variety of forms (scFv, whole, etc.) to bind antigen. For example, Bendig (Methods: A Companion to Methods in Enzymology 1995; 8:83-93) reviews that the general strategy for “humanizing” antibodies involves the substitution of all six CDRs from a rodent antibody that binds an antigen of interest, and that all six CDRs are involved in antigen binding (see entire document, but especially Figures 1-3). Similarly, the skilled artisan recognized a “chimeric” antibody to be an antibody in which both the heavy chain variable region (which comprises the three heavy chain CDRs) and the light chain variable region (which comprises the three light chain CDRs) of a rodent antibody or the human CDRs with other human framework regions are recombined with constant region sequences from a human antibody of a desired isotype (see entire document, but especially Figures 1-3). The state of the art recognized that it would be highly unpredictable that a specific binding member comprising an antibody variable region but comprising less than all six CDRs of a parental antibody with a desired specificity would bind the same antigen as the parental antibody. Thus the minimal structure which the skilled artisan would consider predictive of the function of binding includes six CDRs (three in the heavy chain variable region and three in the light chain variable region) from the same parental antibody in the context of an antibody framework. In addition, the skilled artisan recognized that single CDRs with the same amino acid sequence could be found in antibodies with diverse specificities. In particular, antibodies which have not yet undergone affinity maturation may still utilize germline heavy and light chain sequences. Between antibodies utilizing the same germline heavy or light chain gene the skilled artisan would expect to find that one or more of the heavy and/or light chain CDRs were the same as that of an antibody with a different specificity, particularly CDRs 1and 2 which are germline encoded completely in the variable region. The same CDR may also occur in antibodies having somatic mutations that bind different antigens. Thus it would be highly unpredictable that the instantly recited specific binding member comprised of fewer than all six CDRs (three CDRs defined in the heavy chain variable region and three CDRs defined in the light chain variable region) of a particular reference antibody would have the same specificity as the reference antibody. Further, the antibody structure is not a random combination of heavy and light chain variable regions. The antibody paratope, binds an epitope on an antigen. The paratope of the antibody is highly specific and provides for a specific three-dimensional pocket in which the epitope of the antigen binds. The pocket is dependent on the specific primary structure of the complementary determining regions provided in a framework of other regions in a specific order. The specification does not describe nor enable the random combination of heavy and light chain variable regions or CDR's fragments therefrom to prepare an antibody. The references serve to demonstrate the highly unpredictable nature of substituted antibodies and thus, the highly unpredictable nature of the antibody of the instant claims. Given said unpredictability the skilled artisan would not place Applicants in possession of the genus of antibodies that bind and have random combinations of variable light and variable heavy chains. Possession of a genus may not be shown by merely describing how to obtain members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
In the absence of sufficient recitation of distinguishing characteristics, the specification does not provide adequate written description of the claimed genus of antibody drug conjugates where the antibodies bind nexin4 with no structural form or with highly variant structures that are not supported by the limited disclosure. As such, given the limited disclosure the skilled artisan would be unable or readily envision which antibodies or fragments which have the recited characteristics pointed out above sufficient to describe the antibody portion of the conjugate. One of skill in the art would not recognize from the disclosure that the applicant was in possession of the genus. The specification does not clearly allow persons of ordinary skill in the art to recognize that he or she invented what is claimed (see Vas-Cath at page 1116). Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. 112 is severable from its enablement provision (see page 1115).For all the foregoing reasons, in view of the enormous genus of antibodies, the numerous factors impinging binding and function of the antibodies to the target and also having the specifically claimed function, the lack of description of a representative number of antibodies that function as claimed to even begin to conjugate to amatoxin, the antibodies are not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 2-8 and 11-16 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
As to claims 2-8 and 11-16, the phrases “in particular”, “particularly”, “e.g.” are prima facie indefinite as it is unclear if the recitation of additional limitations are included in the claims or not.
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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1-8 and 11-16 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 2 of U.S. Patent No. 12,049,500 in view of Lutz et al (EP 3222292A1 published 9-27-2017) and Lopez (US 10,675,357, 6-9-2020, with priority to 9-7-2016).
Claim 2 of the ‘500 Patent claims and antibody or antigen binding fragments comprising SEQ ID NO:13(VH) and 14(VL) or percent identical variants which derived from monoclonal antibody 15A7.5 or ch-15A7.5. The patented antibody or fragment thereof which is identical to SEQ ID NO:13 and 14 of the instant claims that inherently comprise the heavy and light chain CDRs recited herein as SEQ ID NO:1-3 and 4-6 respectively. The patented claims differ by not conjugating the antibody of SEQ ID NO:13 and 14 to the cytotoxic drug, amatoxin by a cleavable linker attached to a cysteine amino acid.
Lutz et al teach amatoxin conjugates where an amatoxin, modified alpha-amanitin is conjugated to a targeting moiety (see abstract; page 4, paragraph [0023]). Lutz et al teach that alpha-amanitin is one of the amatoxins particularly suited for conjugation. Lutz et al teach that the targeting moiety may be antibodies or antigen-binding fragments thereof (see paragraph [0030]). Lutz et al teach that target molecules include tumor-associated antigens which are present on the surface of tumor cell types (see paragraph [0032]). Lutz et al teach that the linker by be a stable linker or a cleavable linker (see paragraphs [0053-0057]). Lutz et al teach that the conjugates have use for treating cancer.
Lopez teaches antibodies that bind nexcin-4 (N41, N42, N43, HA22-2 monoclonals) and cytotoxic conjugates thereof (column 17, line 22 to column 18, line 65). Lopez teaches nectin-4 antibody conjugates N41mabvcMMAE and HA22-2vcMMAE (see column 32, line 28 – 37). The linker is a cleavable linker (maleimidocaproyl-L-valine-L-citrullline-paminobenzyl alcohol p-nitrophenyl carbonate covalently conjugated to monomethyl auristatin-E (MMAE). The linker is attached to an antibody cysteine. The drug to antibody ratio was 4.73. Lopez et al demonstrate that the ADC treatment provided marked anti-tumor activity in both nectin-4 expressing primary and metastatic cells (see column 35, line 7-column 36, line 18). Lopez teaches pharmaceutical compositions comprising the conjugates for treatment of cancer. Lopez teaches that the techniques for conjugating molecules to antibodies are well known in the art and typically can be conjugated attached to lysines or cysteines on the antibody through N-hydroxysuccinimide ester or maleimide functionality respectively. Methods of conjugation using engineered cysteines or incorporation of unnatural amino acids have been reported to improve the homogeneity of the conjugate (see column 19, lines 28-55). Inasmuch as the claims encompass unlimited variation of the elected combination of CDRs or the VH or VL the anti-nectin-4 antibodies read on the claimed antibody in the conjugate. The current language of claims 7 and 8 provides for a percent identity to only “an amino acid sequence” which can be any subsequence of SEQ ID NO:13 or 14. Lopez demonstrates that conjugates of anti-nectin-4 antibodies are useful as pharmaceutical agents to treat nectin-4 positive cancers.
It would have been prima facie obvious at the time of filing to modify the nectin-4 antibody of claim 2 of the ‘500 patent by substituting the N41 of the N41mab-2vcMMAE conjugate of Lopez with the claim 2 antibody and then substituting the MMAE cytotoxic agent with the amatoxin/ alpha-amatoxin agent of Lutz et al because Lopez teaches that any cytotoxic agent can be conjugated for a useful therapeutic agent and both Lopez and Lutz et al teach that cytotoxic agents conjugated to antibodies are useful for the treatment of nectin-4 positive cancer.
It is noted that both the ‘500 patent, and the instant application apparently claim priority to the same document EPO 21209332.2.
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 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.
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.
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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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.
Claims 1-5, 7, 8 and 11-16 are rejected under 35 U.S.C. 103 as being unpatentable over Lopez (US 10,675,357, 6-9-2020, with priority to 9-7-2016) in view of Lutz et al (EP 3222292A1 published 9-27-2017).
Lopez teaches antibodies that bind nexcin-4 (N41, N42, N43, HA22-2 monoclonals) and cytotoxic conjugates thereof (column 17, line 22 to column 18, line 65). Lopez teaches nectin-4 conjugates N41mabvcMMAE and HA22-2vcMMAE (see column 32, line 28 – 37). The linker is a cleavable linker (maleimidocaproyl-L-valine-L-citrullline-paminobenzyl alcohol p-nitrophenyl carbonate covalently conjugated to monomethyl auristatin-E (MMAE). The linker is attached to an antibody cysteine. The drug to antibody ratio was 4.73. Lopez et al demonstrate that the ADC treatment provided marked anti-tumor activity in both nectin-4 expressing primary and metastatic cells (see column 35, line 7-column 36, line 18). Lopez teaches pharmaceutical compositions comprising the conjugates for treatment of cancer. Lopez teaches that the techniques for conjugating molecules to antibodies are well known in the art and typically can be conjugated attached to lysines or cysteines on the antibody through N-hydroxysuccinimide ester or maleimide functionality respectively. Methods of conjugation using engineered cysteines or incorporation of unnatural amino acids have been reported to improve the homogeneity of the conjugate (see column 19, lines 28-55). Inasmuch as the claims encompass unlimited variation of the elected combination of CDRs or the VH or VL the anti-nectin-4 antibodies read on the claimed antibody in the conjugate. The current language of claims 7 and 8 provides for a percent identity to only “an amino acid sequence” which can be any subsequence of SEQ ID NO:13 or 14. Lopez differs by not conjugating the N41mab or the HA22-2mab to amatoxin and alpha-amanitin in particular.
Lutz et al teach amatoxin conjugates where an amatoxin, modified alpha-amanitin is conjugated to a targeting moiety (see abstract; page 4, paragraph [0023]). Lutz et al teach that alpha-amanitin is one of the amatoxins particularly suited for conjugation. Lutz et al teach that the targeting moiety may be antibodies or antigen-binding fragments thereof (see paragraph [0030]). Lutz et al teach that target molecules include tumor-associated antigens which are present on the surface of tumor cell types (see paragraph [0032]). Lutz et al teach that the linker by be a stable linker or a cleavable linker (see paragraphs [0053-0057]). Lutz et al teach that the conjugates have use for treating cancer.
It would have been prima facie obvious at the time of filing to modify the N41mabvcMMAE and HA22-2vcMMAE conjugates of Lopez by substituting the MMAE cytotoxic agent with the amatoxin/ alpha-amatoxin agent of Lutz et al because Lopez teaches that any cytotoxic agent can be conjugated and Lutz et al teach that amatoxins are useful cytotoxic agents for conjugation to antibodies for the treatment of cancer.
Claims 1-5, 7, 8 and 11-16 are rejected under 35 U.S.C. 103 as being unpatentable over Lopez et al (WO 2018/158398; of record) in view of Lutz et al (EP 3222292A1 published 9-27-2017).
Lopez teaches antibodies that bind nexcin-4 (14A5.2 and HA22-2 monoclonals) and cytotoxic conjugates thereof (page 32, line 30-page 35, line 9, line 27). Lopez et al teach antibody 14A5.2 conjugated to a cytotoxic agent (see claim 7, page 59). The monoclonal antibodies are conjugated by a linker which may be cleavable by a cleaving agent such as an enzyme or are pH sensitive (see page 35, line9- page 36, line 20). Techniques for conjugation are well known to the art. Lopez et al teach pharmaceutical compositions in effective amounts at page 40-41 for the treatment of cancers (page 50, line 25 – page 53, line 15). Lopez teaches nectin-4 conjugates 14A5.2mabvcMMAE and HA22-2vcMMAE (see pages 54 last paragraph to 57, line 4). The linker is a cleavable linker (maleimidocaproyl-L-valine-L-citrullline-paminobenzyl alcohol p-nitrophenyl carbonate covalently conjugated to monomethyl auristatin-E. The drug to antibody ratio was approximately 4 (see page 55, line 5-6). Lopez et al demonstrate that the ADC treatment provided marked anti-tumor activity in both nectin-4 expressing primary and metastatic cells. Inasmuch as the claims encompass unlimited variation of the elected combination of CDRs, or the VH or VL, the anti-nectin-4 antibodies read on the claimed antibody in the conjugate. The current language of claims 7 and 8 provides for a percent identity to only “an amino acid sequence” which can be any subsequence of SEQ ID NO:13 or 14. Lopez et al differ by not conjugating the14A5.2mab or the HA22-2vcMMAE to amatoxin and alpha-amanitin in particular.
Lutz et al teach amatoxin conjugates where an amatoxin, modified alpha-amanitin is conjugated to a targeting moiety (see abstract; page 4, paragraph [0023]). Lutz et al teach that alpha-amanitin is one of the amatoxins particularly suited for conjugation. Lutz et al teach that the targeting moiety may be antibodies or antigen-binding fragments thereof (see paragraph [0030]). Lutz et al teach that target molecules include tumor-associated antigens which are present on the surface of tumor cell types (see paragraph [0032]). Lutz et al teach that the linker by be a stable linker or a cleavable linker (see paragraphs [0053-0057]). Lutz et al teach that the conjugates have use for treating cancer.
It would have been prima facie obvious at the time of filing to modify the 4A5.2mabvcMMAE, N41mabvcMMAE and HA22-2vcMMAE conjugates of Lopez by substituting the MMAE cytotoxic agent with the amatoxin/ alpha-amatoxin agent of Lutz et al because Lopez teaches that any cytotoxic agent can be conjugated and Lutz et al teach that amatoxins are useful cytotoxic agents for conjugation to antibodies for the treatment of cancer.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Patricia Duffy whose telephone number is (571)272-0855. The examiner can normally be reached 8:00 am - 4 pm.
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/Patricia Duffy/Primary Examiner, Art Unit 1645
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