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 .
Status of the Claims
Claims 1, 45, 49, 52-53, 55, 57, 59-60, 65, and 70 are pending and examined herein.
Priority
This application, filed 04/03/2024, is a 371 of PCT/US2022/045633, filed 10/04/2022, which claims benefit of PRO 63/299,104, filed 01/13/2022, and PRO 63/252,245, filed 10/05/2021.
Information Disclosure Statement
The Information Disclosure Statements filed 02/27/2025 and 10/29/2025 are acknowledged and have been considered.
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 70 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 70 recites “A method of modifying the level of FcγRII binding of an antibody composition, comprising a) specifying a level of FcγRII; and b) modifying the level of [glycans]…to achieve the specified level of FcγRII.” As claimed, the method would require manipulation of FcγRII protein levels, which are not present in an antibody composition. The invention does not seem to be directed toward modifying the levels of FcγRII itself, but the levels of FcγRII binding. For purposes of compact prosecution, the claim will be interpreted to mean specifying a level of FcγRII binding and achieving the specified level of FcγRII binding; however, appropriate correction or clarification is requested.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 45, 49, 52-53, 57, 59-60, and 65 are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by WO 2019/236739 A1 “MODULATING ANTIBODY DEPENDENT CELLULAR PHAGOCYTOSIS” (published 12/12/2019, IDS dated 02/27/2025, referred to herein as Kuhns).
Regarding claims 1 and 52, Kuhns teaches a method of determining product quality of an antibody composition, i.e. determining the factors that affect ADCP, (para. 00166, lines 1-6) and producing an antibody composition (para. 0025, lines 1-2) comprising determining the afucosylated (Example 3, para. 00187) or β-galactosylated glycan content (Example 2, para. 00182, lines 1-3). Kuhns teaches calculating FcγRII binding based on β-galactosylated content (para. 00185, lines 1-5). Kuhns teaches determining the product quality as acceptable when the ADCP activity is at a target level within a range by altering the β-galactose levels (para. 0009, lines 1-12). At the same time, Kuhns teaches that ADCP activity is due to differences in FcγRII binding as a result of β-galactose levels (Figure 9, para. 0037, lines 1-5); therefore, Kuhns teaches determining the product quality of the antibody composition as acceptable when the β-galactose content is within a target range.
Regarding claim 45, Kuhns teaches determining the quality of the composition with a first and second sample at different time points (para. 0009, lines 24-27).
Regarding claims 49, 59, and 60 Kuhns teaches altering the afucosylated or β-galactosylated content by modifying culture conditions to alter the glycosylation levels to determined levels, i.e. within a target range (para. 0024, lines 1-6).
Regarding claim 53, Kuhns teaches producing a chimeric antibody (para. 00135, lines 1-7).
Regarding claim 57, Kuhns teaches the samples is of a cell culture comprising glycosylation-competent cells expressing an antibody (para. 00106, lines 1-8).
Regarding claim 65, Kuhns teaches determining the product quality as acceptable when the ADCP activity is at a target level (para. 0009, lines 1-12).
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.
Claim 55 is rejected under 35 U.S.C. 103 as being unpatentable over Kuhns in view of Strohl, “Optimization of Fc-mediated effector functions of monoclonal antibodies” Current Opinion in Biotechnology (published 11/04/2009, referred to herein as Strohl).
The teachings of Kuhns, as applied to claim 52, above, is incorporated herein.
Regarding claim 55, Kuhns teaches a method of producing an antibody composition (para. 0025, lines 1-2) by evaluating the binding to FcγRII (Figure 9, para. 0037, lines 1-5) with chimeric antibodies (para. 00135, lines 1-4).
However, Kuhns does not teach the specific use of antibodies comprising CH1 of an IgG2 and/or CH2-CH3 of an IgG4.
Strohl teaches that it is important to evaluate the Fc receptor functionality of eculizumab (p. 687, col. 2, para. 1, lines 1-8), which is an antibody comprising the CH1 domain of an IgG2 and the CH@-CH3 domains of an IgG4 (Instant Specification, para. 00125, lines 11-14).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the method taught by Kuhns to evaluate the Fc receptor binding of eculizumab, as taught by Strohl. An artisan would have been motivated to evaluate eculizumab because, as taught by Strohl, the Fc binding activity, or lack thereof, of eculizumab is important for its therapeutic effect; therefore, evaluation of Fc binding would ensure its therapeutic potential. An artisan would have a reasonable expectation of success in evaluating eculizumab Fc binding using the methods of Kuhns because the method is directed towards the evaluation of Fc binding of monoclonal antibodies via their constant region, which is a known important mechanism of eculizumab action.
Claim 70 is rejected under 35 U.S.C. 103 as being unpatentable over Kuhns.
Regarding claim 70, Kuhns teaches a method of modifying the ADCP activity of an antibody composition comprising specifying a level of ADCP activity and modifying the level of afucosylated or β-galactosylated glycans of the antibody composition (para. 00147, lines 7-15). Kuhns teaches that the changes in ADCP activity after modulation of glycan levels is due to changes in FcγRII binding (para. 0037, lines 3-5).
However, Kuhns does not teach a step of specifying a level of FcγRII.
It would have been obvious to one of skill in the art before the effective filing date of the claimed invention to modify the method taught by Kuhns by substituting the target ADCP activity for a target level of FcγRII binding by modifying the levels of glycans. An artisan would have been motivated to make this change with a reasonable expectation of success in order to ensure that the antibody composition is able to successfully enable FcγRII binding-dependent ADCP, which is an important molecular mechanism for the antibody composition, as taught by Kuhns.
Conclusion
No claims are allowable.
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/C.E./Examiner, Art Unit 1677
/BAO-THUY L NGUYEN/Supervisory Patent Examiner, Art Unit 1677 August 5, 2026
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