DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Applicant’s election without traverse of Group I and species of IL-31 in the Response filed on January 5, 2026 is acknowledged.
Claims 1-45 have been canceled.
Claims 44-57 are pending.
Claims 48 and 51-57 have been withdrawn under 37 CFR 1.142(b) as being drawn to nonelected invention/species.
Claims 44-47, 49, and 50 are currently under consideration as they read on the elected invention.
3. 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.
4. 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.
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.
5. Claims 44-46, 49, and 50 are rejected under 35 U.S.C. 103 as being unpatentable Leger (WO 2018/073185, reference on IDS) in view of Adam (US 2006/0067930, reference on IDS).
Leger et al. teach a canine IgG Fc domain comprising amino acid substitutions (e.g. see Abstract and page 8). Leger et al. teach the amino acid sequences of the wild type canine IgB, IgD, and IgA (e.g. see Figure 8). Leger et al. teach a canine IgG Fc domain having increased binding affinity to canine FcRn compared to the parent canine IgG without amino acid substitution (e.g. see page 7). Leger et al. identified N434 as one of the seven residues belonging to the binding interface of the native canine Fc/FcRn complex (e.g. see Figure 8 and its legend in page 33). N434 is conserved between all canine IgG and human IgG.
Leger et al. teach that human Fc variants comprising M252Y/S254T/T256E (the YTE mutant) and H433K/N434F/Y436H were known in the art to improve IgG1-huamn FcRn complex stability (e.g. see page 3). Leger et al. teach full length antibody (e.g. in page 12) which would be understood as encompassing six CDRs.
Leger et al. teach examples of a canine IgG B Fc variant having the YTE (adopted from human YTE) substitutions in the Fc region and show that the Fc variant displayed increase binding to FcRn at pH6.0 as compared to the parent Fc (e.g. see page 4 and Examples in pages 33-49).
Leger et al. teach examples of a canine IgG B Fc variant consists of N114A substitution (corresponding to N434A in EU numbering) in Example 2 in page 37 and shows that this Fc variant binds canine FcRn better than wild type IgG (e.g. see page 38). Ledger et al. teach that the antibody variant can be purified with sodium citrate buffer and neutralized suing Tris buffer and dialyzed into PBS, a well-known pharmaceutically acceptable excipient (e.g. see lines 15-25 in pages 18, 31, and 35).
The reference teachings differ from the instant invention by not describing His at position 434 of the canine IgG Fc region.
Adam et al. teach an antibody comprising a human IgG Fc wherein the amino acid residue N434 is substituted with amino acid residue Trp (W), Tyr (Y), or His (H), wherein the Fc region has higher affinity than native unmutated IgG Fc sequence at pH6.0 (e.g. see claim 72 and FIGs. 8 and 13). Adam et al. further teach that the Fc can be from dog (e.g. see [0138]). Adam further teaches that the antibody can be formulated into a pharmaceutical composition comprising a pharmaceutically acceptable excipient (e.g. see [0053]).
It would thus be obvious to one of ordinary skill in the art at the time the invention was filed to produce a canine IgG B antibody Fc variant by performing amino acid substitution in position 434 to replace the naturally occurring amino acid residue asparagine (N, conserved in human and canine) with histidine for increased binding to FcRn. An ordinary skill in the art would have been motivated to do so, and have a reasonable expectation of success, since Adam et al. and Leger et al. both teach Fc variant comprising amino acid substitution in position N434 in human IgG1 Fc region could enhance the Fc’s affinity to FcRn and Adam teaches human IgG Fc consisting of N434H substitution result in an Fc variant with enhanced affinity to FcRn. Such canine antibody Fc variant would be expected to have the benefit of prolonged serum half life.
Given that Leger teaches that canine IgG B YTE mutant was shown to have the same effect of enhanced binding to FcRn as what was shown in human IgG1 Fc variant comprising YTE mutant, and since Leger teaches that N434 is conserved in canine IgG B (as the human IgG1 Fc region), an ordinary skill in the art would have been motivated to mutate amino acid residues in position N434 with amino acid residues H in the canine anti- Ig B antibody Fc region following well-established point mutation methods as shown in Adam and Leger, with a reasonable expectation of success to produce an canine IgB Fc variant comprising/consisting of amino acid substitution N434H.
Such canine Ig B antibody Fc variant would be expected to inherently/intrinsically exhibit the function of binds to a canine FcRn at higher level at an acidic pH than at a neutral pH and suitable for veterinary use.
6. Claim 47 is rejected under 35 U.S.C. 103 as being unpatentable over Leger (WO 2018/073185) in view of Adam (US 2006/0067930) as applied to claims 44 and 45 above, and further in view of Li (WO 2018/156180, reference on IDS).
The teachings of Leger and Adam have been discussed above.
The teachings of Leger and Adam differ from the instant invention by not teaching a binding domain that binds IL-31 (the elected species).
Li teaches that IL-31 is a cytokine mostly produced by Th2 cells and is involved in promoting skin diseases such as atopic dermatitis in humans and dogs (e.g. see [0003]-[0004]). Li teaches an anti-canine IL-31 antibody and method of treating atopic dermatitis by administering to the animal an effective amount of the antibody (e.g. see [0022] and claims 1-43). Li teaches working examples of anti-canine IL-31 antibody comprising a canine constant heavy chain IgG B and canine constant light chain (e.g. see [00129]-[00130]).
It would thus be obvious to one of ordinary skill in the art at the time the invention was filed to produce a canine anti-IL-31 antibody IgG B antibody Fc variant by performing amino acid substitution in position 434 to replace the naturally occurring amino acid residue asparagine (N, conserved in human and canine) with histidine for increased binding to FcRn.
An ordinary skill in the art would have been motivated to do so, and have a reasonable expectation of success, since Adam et al. and Leger et al. both teach Fc variant comprising amino acid substitution in position N434 in human IgG1 Fc region could enhance the Fc’s affinity to FcRn and Adam teaches human IgG Fc consisting of N434H substitution result in an Fc variant with enhanced affinity to FcRn. Such anti-IL-31 antibody Fc variant would be expected to have the benefit of prolonged serum half life when administered to dog.
Given that Leger teaches that canine IgG B YTE mutant was shown to have the same effect of enhanced binding to FcRn as what was shown in human IgG1 Fc variant comprising YTE mutant, and since Leger teaches that N434 is conserved in canine IgG B (as the human IgG1 Fc region), an ordinary skill in the art would have been motivated to mutate amino acid residues in position N434 with amino acid residues H in the known canine anti-IL-31 Ig B antibody Fc region taught by Li following well-established point mutation methods as shown in Adam and Leger, with a reasonable expectation of success to produce an canine IgB Fc variant comprising/consisting of amino acid substitution N434H.
7. 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.
8. Claims 44-47, 49, and 50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 4 and 5 of copending USSN 18/427,146 (reference application).
The instant claims are drawn to a polypeptide comprising a canine IgG Fc region variant differ from wild type canine IgG Fc in no more than one amino acid difference of His at position 434.
The claims in the reference application are drawn to a method of treating atopic dermatitis in a canine by administering a polypeptide comprising immunoglobulin antigen binding domain that binds IL-31 and a canine IgG Fc region that differs from the wild type canine IgG Fc region of SEQ ID NO:10 by no more than one amino acid of His at position 434.
Although the claims at issue are not identical, they are not patentably distinct from each other because both instant claims and the claims in the reference application are drawn to the same or nearly the same canine IgG Fc variant with identical amino acid His at position 434. As such, the species of the anti-IL31 canine IgG antibody with identical His at position 434 in the Fc region would anticipate the genus of a polypeptide comprising a canine IgG Fc region with His at position 434.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
9. No claim is allowed.
10. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHUN DAHLE whose telephone number is (571)272-8142. The examiner can normally be reached Mon-Fri 6:30am-4:00pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu can be reached at 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/CHUN W DAHLE/Primary Examiner, Art Unit 1641