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 .
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.
Status of Claims
Claims 1-2, 6-7, 24, 29-40, 44 and 46-53. Claims 32-39 are withdrawn. Claims 1-2, 6-7, 24, 29-31, 40, 44 and 46-53 are under examination.
Withdrawn Rejections
In light of the amendments, the 35 U.S.C. 102(a)(1) rejection over Lu et al. is hereby withdrawn.
In light of the canceled claims 29, 31-32 and 34 in copending Application 17996557, the nonstatutory double patenting rejection is hereby withdrawn.
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.
Claims 40 and 44 are 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.
Amended claims 40 and 44 recite the limitation of a variant IgG Fc polypeptide comprising an amino acid sequence with at least 98% sequence identity to SEQ ID NO: 14, wherein said variant IgG Fc polypeptide comprises an amino acid substitution at position 83 and/or position 208 of SEQ ID NO: 14 is unclear to the metes and bounds of the claimed variant IgG Fc polypeptide. Because the recitation of “wherein said variant IgG Fc polypeptide comprises an amino acid substitution at position 83 and/or position 208 of SEQ ID NO: 14” is not referring back to an amino acid sequence with at least 98% sequence identity to SQ ID NO: 14, it is unclear to whether the substitution at position 83 and/or 208 produces “an amino acid sequence with at least 98%” or referring to a different sequence of the variant IgG Fc polypeptide containing SEQ ID NO: 14 with the substitution. Note that the claims use comprising which is an open-ended recitation.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-2, 6-7, 24, 29-31, 40, 44 and 46-53 are rejected under 35 U.S.C. 103 as being unpatentable over Lu et al. (US2018/0009869, Appl. No. 15644764, published 01/11/2018).
With respect to claims 1 and 31, Lu teaches fusion proteins having an amino acid sequence of 100% to SEQ ID NO:48 (see para. [0019] and Fig. 18). Meanwhile, Lu’s SEQ ID NO: 48 has at least 99% sequence similarity to the claimed SEQ ID NO: 14 (see below). Additionally, SEQ ID NO: 48 does comprise a tyrosine (Y) at position 24 of the instant SEQ ID NO: 14. Lu also teaches in para. [0019] that the fusion protein is believed to further increase the half-life of leptin through introduction of mutations to Fc domain of the fusion protein and increase the binding affinity to Fc receptor FcRn. Lu teaches that Fig. 4 is a schematic illustration of a Canine IgGB Fc leptin fusion molecule (also see para. [0032]). Lu teaches shows amino acid sequences of IgG Fc and analogs in different species (see para. [0041]).
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SEQ ID NO:48 differs at positions at 26 and 28 of instant claimed SEQ ID NO: 14. Meanwhile, Lu does teach that SEQ ID NO: 48 and SEQ ID NO: 47 are Fc-Leptin fusion protein with at least 99% match and mismatched in 3 amino acid positions (see Emphasis below at positions 24, 26, and 28). Additionally, SEQ ID NO: 47 of Lu differs from the claimed variant IgG Fc polypeptide comprising SEQ ID NO: 14 is tyrosine (Y) at position 24 (see claims 1 and 31) but has the same amino acid residues at positions 26 and 28 of the instant claimed SEQ ID NO:14.
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Although Lu discloses that SEQ ID NO: 48 and SEQ ID NO; 47 and each is at least 99% identical to the instant claimed SEQ ID NO: 14, Lu does not teach the variant IgG Fc polypeptide comprising 100 % SEQ ID NO: 14.
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have produced the claimed variant IgG Fc polypeptide from Lu’s SEQ ID NO: 48 and SEQ ID NO: 47 because said sequences of Lu are analogs of Fc-Leptin fusion proteins which contain at least 99% sequence similarity (see above) and differ uniquely at three amino acid positions. Therefore, it would have been obvious to have modified SEQ ID NO: 47 with tyrosine at position 24 because Lu teaches in SEQ ID NO: 48 position 24 (as claimed) was substituted with tyrosine. Meanwhile, it would have been obvious to have used the sequences of the Fc-Leptin fusion analogs as taught by Lu and produced the claimed SEQ ID NO: 14 because (1) there are only three unique amino acids to be modified and (2) SEQ ID NO: 47 only differs at tyrosine of position 24 of the instant variant IgG Fc polypeptide comprising or consisting SEQ ID NO: 14.
With respect to claim 2, as stated above, Lu teaches the claimed polypeptide which would produce the claimed function of increased serum half-life relative to a polypeptide comprising a wild-type Fc polypeptide.
With respect to claim 6, Lu teaches that Fig. 4 is a schematic illustration of a Canine IgG-B Fc leptin fusion molecule, which read on a polypeptide comprising a variant IgG Fc polypeptide (also see para. [0032]).
With respect to claim 7, as stated above, Lu teaches the variant IgG Fc polypeptide is at least 98% identical to SEQ ID NO: 14. Lu teaches that the fusion protein is believed to further increase the half-life of leptin through introduction of mutations to Fc domain of the fusion protein and increase the binding affinity to Fc receptor FcRn (see para. [0019]) which would read on the variant Fc polypeptide binds to FcRn. Note that the recitation of “is at least 98% identical” is interpreted that a sequence that is at least 98% local match to SEQ ID NO: 14 would read on the claims even though the prior art sequence may contain other amino acid residues because these claims recite a polypeptide comprising (open-ended) a variant IgG Fc polypeptide.
As stated above, Lu teaches the claimed polypeptide structure, which would read on the functional language of affinity greater than the wild-type IgG Fc polypeptide. The limitations of as measured by biolayer interferometry at a pH in the range of from at about 5.0 to about 6.5 are directed to intended use because the claims are directed to a polypeptide. Because the prior art teaches all the structural limitations of the claimed polypeptide, the Lu’s polypeptide is capable of measuring the intended use. When a prior art recites all the structural limitations of the claimed sequence, then the prior art sequence is capable for the intended use.
With respect to claim 24, Fig. 4 shows the polypeptide is an antibody, an antibody fragment, or a fusion polypeptide.
With respect to claim 29, as stated above, Lu teaches the variant IgG Fc polypeptide is at least 98% identical to SEQ ID NO: 14. Fig. 4 shows a canine IgG-B Fc polypeptide, which would bind to canine and/or feline IL31.
With respect to claim 30, as stated above, Lu teaches the variant IgG Fc polypeptide is at least 99% identical to SEQ ID NO: 14. Fig. 4 shows a canine IgG-B Fc polypeptide, which would produce the claimed binding affinity.
With respect to claims 40 and 44, as stated above, Lu does not teach amino acid substitution at position 83 and/or position 208 of SEQ ID NO: 14. However, it would have been obvious to have substituted tyrosine at position 83 or 208 because Lu teaches in SEQ ID NO: 48 position 24 (as claimed) was substituted with tyrosine.
With respect to claim 46, the recitation of “consists of SEQ ID NO: 14” is interpreted that a sequence that locally has SEQ ID NO: 14 (i.e., without gap) would read on the claim even though the prior art sequence may contain other amino acid residues because the claim recites a polypeptide comprising (open-ended) the variant IgG Fc polypeptide consists of SEQ ID NO: 14.
With respect to claims 47-48 and 50-51, the recitation of “is linked to a variable heavy chain polypeptide that binds to canine” is intended use. Because the prior art teaches all the structural limitations of the claimed variant IgG Fc polypeptide, the prior art polypeptide is configured and capable of performing the intended use. When a prior art recites all the structural limitations of the recited variant IgG Fc polypeptide, then the prior art polypeptide has the structure that is capable for the intended use.
With respect to claims 49 and 52-53, as stated above, Lu’s polypeptides read on the claimed polypeptide. Additionally, Lu teaches that Fig. 4 is a schematic illustration of a Canine IgG-B Fc leptin fusion molecule, which read on a polypeptide comprising a variant IgG Fc polypeptide (also see para. [0032] and SEQ ID NO: 48). Thus, Lu’s polypeptides would bind to FcRn with the claimed function.
Response to Arguments
Applicant's arguments filed 03/23/2026 have been fully considered but they are not persuasive.
35 U.S.C. 112b rejection:
Applicant argues that claim 40 has been amended to overcome the indefiniteness issue.
The argument is not found persuasive for the reasons stated above in the 112b rejection. The rejection has been modified in view of the amendments.
35 U.S.C. 103 rejection:
Applicant argues on page 9 that Lu does not teach an amino acid sequence with 100% sequence identity to SEQ ID NO: 14 and Lu’s SEQ ID NOs 47 and 48 also lack a substitution at amino acid position 83 and/or position 208. Applicant further argues that the claimed polypeptides have superior and unexpected results.
With regarding to unexpected results, the arguments are not found persuasive because Applicant has not provided evidence that commensurate in scope with the claimed subject matter. To show unexpected results, the evidence must be (1) commensurate in scope with the claimed subject matter, In re Clemens, 622 F.2d 1019, 1035, 206 USPQ 289, 296 (CCPA 1980), (2) show what was expected, to "properly evaluate whether a … property was unexpected", and (3) compare to the closest prior art. Pfizer v. Apotex, 480 F.3d 1348, 1370-71, 82 USPQ2d 1321, 1338 (Fed. Cir. 2007). To invoke unexpected and superior results, the claimed method needs to be commensurate in scope with the cited specification. In particular, the data from the specification (reproduced in the Remarks) require at least the substitution of tyrosine at position 208 with respect to SEQ ID NO: 14 (i.e., SEQ ID NOs: 33-47 and 50-51 of specification). However, the independent claims 1 and 40 are not commensurate in scope with the unexpected results as disclosed in the specification.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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