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 .
Response to Amendment
Applicant’s amendment filed 07/07/2026 is acknowledged. Claims 1, 2, 4, 7, 13-17 and 19 are amended and claims 3 and 18 are canceled. 1, 2, 4-17, 19 and 20 are under examination.
Claim Objections
Claims 2 and 4 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Objections/Rejections Withdrawn
Any previous rejections over claims 3 and 18 are hereby withdrawn in response to Applicant’s cancelation of those claims.
Specification
The objection to the disclosure for containing an embedded hyperlink and/or other form of browser-executable code is withdrawn in response to Applicant’s amendment to the specification filed 07/07/2026 removing the embedded hyperlinks from paragraphs [0062] and [0095].
Claim Rejections - 35 USC § 112(b)
The rejection of claims 7 and 17 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or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in response to Applicant’s amendment. Specifically, claim 7 has been amended to delete reference to the registered trademark name ForteBio®. Further, claim 17 has been amended to recite active positive steps (see MPEP 2173.05(q)).
Claim Rejections - 35 USC § 112(a)
Scope of Enablement
The rejection of claims 2 and 4 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, for scope of enablement is withdrawn in response to Applicant’s amendment of these claims to be limited to antibodies set forth in the statement of enablement at pages 4-5 of the Office action mailed 04/07/2026. Further, the variable language has been removed from claim 4.
Written Description
The rejection of claims 2 and 4 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in response to Applicant’s amendment of these claims to be limited to antibodies set forth in the statement of enablement at pages 4-5 of the Office action mailed 04/07/2026. Further, the variable language has been removed from claim 4.
Rejections Maintained
Claim Rejections - 35 USC § 112(a)
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 the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Scope of Enablement
The rejection of claims 1, 5-17, 19 and 20 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, for scope of enablement is maintained for reasons or record and the following. Applicant’s amendment to claim 1 is acknowledged, however, the encompassed antibodies still represent 8 possible variations for LCDR1, 2 possible variations for LCDR2, 6 possible variations for HCDR1, 2 possible variations for HCDR2 and 192 possible variations for HCDR3 for a total of 36,864 possible combinations. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims.
Response to Arguments
Applicant argues at p. 22 of the Remarks filed 07/07/2026 that the claim 1 has been amended to incorporate the limitations of now canceled claim 3, which was not rejected under 35 USC 112(a). Further, Applicant argues that claim 1 not directed to random mutagenesis, but rather delineates a finite set of acceptable amino acid substitutions.
This argument has been fully considered, but is not found persuasive. Applicant incorporated part of the limitations in now canceled claim 3, but not the portion that limited the claims to light chain complementarity determining regions (LCDRs) and heavy chain complementarity determining regions (HCDRs) comprising:
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; and HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 4; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 11;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 5 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 12; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 13;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 6 and LCDR3 comprising an amino acid sequence of SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 14; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 15;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 16;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 17;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 18;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2; LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 19;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 7; LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 20; HCDR2 comprising SEQ ID NO: 21 and HCDR3 comprising SEQ ID NO: 10;
The elements of canceled claim 3 that rendered it enabled, namely parts (i)-(xii), were not incorporated into now amended claim 1. As a result, the encompassed antibodies still represent 8 possible variations for the LCDR1, 2 possible variations for the LCDR2, 6 variations for HCDR1, 2 possible variations for HCDR2 and 192 possible variations for HCDR3 or 36,864 possible combinations.
The state of the art teaches antibody variable regions are composed of a heavy and light chain, each involved in providing for binding specificity. Predicting antibody amino acid substitutions while maintaining functionality is complex. The art teaches that small changes in the amino acid structure of the CDRs can have large effects on activity. For instance, Piche-Nicholas et al. (MAbs. 2018; 10: 81-94. doi: 10.1080/19420862.2017.1389355) teach that the “binding affinity of IgG
Molecules…to FcRn that differed by only a few amino acid residues in CDRs revealed
that small changes in CDRs, as minute as one amino acid residue change, could alter
affinity to FcRn up to 79-fold.” See p. 89, right column, last paragraph of Piche-Nicholas et al. In the instant case, however, the claims allow for swapping heavy and light chains for a total of 512 combinations in addition to a diversion from the recited CDRs by ~17-29%. Claim 4 compounds this because it recites up to 15% diversion from the recited heavy and light chains. Townsend et al. (Frontiers in Immunology, 7, 388 2016) teach “[v]ariability in the antigen binding site is achieved by V(D)J recombination via heavy and light chain pairing”, with the “most diverse” regions being the 6 CDR regions in the heavy and light chain. While the heavy chain is the most diverse, light chains are also important for binding specificity of antibodies, swapping light chains can “change the antigen specificity of the antibody” (see paragraph bridging pages 1-2). Furthermore, the light chain repertoire is extremely diverse being encoded by kappa and lambda gene segments, each with different V and J genes (see Townsend, p. 2, left column, 1st two paragraphs; p. 4, right column, 1st paragraph). Furthermore, the diversity of the immunoglobulin repertoire is mediated in part by different combinations of heavy and light chain V regions that pair to form a unique antibody binding site. See, for example, Rabia et al. (Biochem. Engin. J. 137, 365-374, 2018), which teaches that “the maximal chemical diversity of antibody CDRs is unimaginably large…[and] it is extremely challenging to define the sequence determinant of antibody specificity” (see p. 368 left column, 4th paragraph). Thus, the screening all of the possible anti-CD40 antibody variants for the recited functions, including preventing and treating tumors or infectious disease would require an undue amount of experimentation.
Due to the large quantity of experimentation necessary to test the variant antibodies for the ability to prevent/treat any cancer or infectious disease, the lack of direction/guidance presented in the specification regarding the same and the absence of working examples directed to the same, the complex nature of the invention, the unpredictability of the effects of mutation on antibody binding and function, and the breadth of the claims which fail to recite limitations on the antibodies or the patient population, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope.
Written Description
The rejection of claims 1, 5-17, 19 and 20 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is maintained for reasons of record and the following. Applicant’s amendment to claim 1 is acknowledged, however, the encompassed antibodies still represent 8 possible variations for the LCDR1, 2 possible variations for the LCDR2, 6 variations for HCDR1, 2 possible variations for HCDR2 and 192 possible variations for HCDR3. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims.
Response to Arguments
Applicant argues at p. 22 of the Remarks filed 07/07/2026 that the claim 1 has been amended to incorporate the limitations of now canceled claim 3, which was not rejected under 35 USC 112(a). Further, Applicant argues that claim 1 not directed to random mutagenesis, but rather delineates a finite set of acceptable amino acid substitutions.
This argument has been fully considered, but is not found persuasive. Applicant incorporated part of the limitations in now canceled claim 3, but not the portion that limited the claims to light chain complementarity determining regions (LCDRs) and heavy chain complementarity determining regions (HCDRs) comprising:
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; and HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 4; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 11;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 5 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 12; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 13;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 6 and LCDR3 comprising an amino acid sequence of SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 14; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 15;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 16;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 17;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 18;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2; LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 19;
LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 7; LCDR3 comprising SEQ ID NO: 3; HCDR1 comprising SEQ ID NO: 20; HCDR2 comprising SEQ ID NO: 21 and HCDR3 comprising SEQ ID NO: 10;
The elements of canceled claim 3 that were described in the application as originally filed, namely parts (i)-(xii), were not incorporated into now amended claim 1. As a result, the encompassed antibodies still represent 8 possible variations for the LCDR1, 2 possible variations for the LCDR2, 6 variations for HCDR1, 2 possible variations for HCDR2 and 192 possible variations for HCDR3 for a total of 36,864 possible combinations.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. The prior art teaches that small changes in the amino acid structure of the CDRs can have large effects on activity. For instance, Piche-Nicholas et al. (MAbs. 2018; 10: 81-94. doi: 10.1080/19420862.2017.1389355) teaches that the “binding affinity of IgG Molecules…to FcRn that differed by only a few amino acid residues in CDRs revealed that small changes in CDRs, as minute as one amino acid residue change, could alter affinity to FcRn up to 79-fold.” See p. 89, right column, last paragraph of Piche-Nicholas et al. In the instant case, however, very large changes in amino acid sequence of the CDRs is encompassed by the scope of the claims.
Townsend et al. (Frontiers in Immunology, 7, 388 2016) teach “[v]ariability in the antigen binding site is achieved by V(D)J recombination via heavy and light chain pairing”, with the “most diverse” regions being the 6 CDR regions in the heavy and light chain. While the heavy chain is the most diverse, light chains are also important for binding specificity of antibodies, swapping light chains can “change the antigen specificity of the antibody” (see paragraph bridging pages 1-2). Furthermore, the light chain repertoire is extremely diverse being encoded by kappa and lambda gene segments, each with different V and J genes (see Townsend, p. 2, left column, 1st two paragraphs; p. 4, right column, 1st paragraph). Furthermore, the diversity of the immunoglobulin repertoire is mediated in part by different combinations of heavy and light chain V regions that pair to form a unique antibody binding site. See, for example, Rabia et al. (Biochem. Engin. J. 137, 365-374, 2018), which teaches that “the maximal chemical diversity of antibody CDRs is unimaginably large…[and] it is extremely challenging to define the sequence determinant of antibody specificity” (see p. 368 left column, 4th paragraph). In summary, given that the art is not reasonably predictable, the 12 species disclosed in the instant specification are not representative of the over 500 possible antibodies in addition to substitutions of between ~17-29% of the variable regions, including CDRs. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) 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). With the exception of the 12 antibodies disclosed at pages 53-56 of the instant specification, the skilled artisan cannot envision the detailed chemical structure of the encompassed polypeptides, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Therefore, only the 12 antibodies disclosed at pages 53-60 of the instant specification, but not the full breadth of the claim meets the written description provision of 35 U.S.C. §112, first paragraph. 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).
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.
The provisional rejection of claims 1, 2, 4-17, 19 and 20 on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of copending Application No. 18/715,119 (reference application) is maintained for reasons of record and the following.
Response to Arguments
Applicant argues at p. 23 that since the effect US filing date of the instant application is earlier than that of the copending reference application, the rejection should be withdrawn if it is the only rejection of record left in the application, citing MPEP 804.
This argument has been fully considered, but is not found persuasive. While the examiner has no issue with the citation from the MPEP, the provisional rejection is not the only remaining rejection of record, and therefore, should be maintained.
Conclusion
Claims 1, 5-17, 19 and 20 are rejected and claims 2 and 4 are objected to.
THIS ACTION IS MADE FINAL. 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA M BORGEEST whose telephone number is (571)272-4482. The examiner can normally be reached M-F 9-5:30 EDT.
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/CHRISTINA M BORGEEST/Primary Examiner, Art Unit 1675
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