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 .
Claims 21, 24, 28 and 41 are pending and being acted upon in this Office Action.
Priority
Applicant’ claim priority to provisional application 63/614,765, filed December 26, 2023, is acknowledged.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on January 29, 2026, January 14, 2026 and September 25, 2025 have been considered by the examiner and an initialed copy of the IDS is included with this Office Action.
Rejection Withdrawn
The written description and enablement rejections of claims 21-40 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph are withdrawn in view of the claim amendment and the arguments at p. 9-18.
The rejection of claims 20-40 on the ground of nonstatutory double patenting as being unpatentable over claims 15-21 of US Patent 12,364,777 (reference) is withdrawn in view of the claim amendment.
The provisional rejection of claims 20-40 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 9-20 of copending Application No. 18/821,708 (reference application) is withdrawn in view of the claim amendment.
The provisional rejection of claims 20-40 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-9, 11-14, 17, 19-20 of copending Application No. 18/807,087 (reference application) in view of Braslawsky et al. (US Patent 6,897,044) is withdrawn in view of the argument that Braslawsky teaches away from the S444C substitution and cannot motivate substituting S444 for S119.
The provisional rejection of claims 20-40 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-11, 14, 16-20 of copending Application No. 18,807,097 (reference application, will be 12371494) in view of Braslawsky (US Patent 6,897,044) is withdrawn in view of the argument that Braslawsky teaches away from the S444C substitution and cannot motivate substituting S444 for S119.
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 21, 24, 28 and 41 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 applicant regards as the invention.
Claim 21 recites “S444”, “S444C”, “F405L”, “K409R”, but the claims fail to provide any frame of reference that would allow one of skill in the art to unambiguously identify the positions being referred to in the IgG. Accordingly, one skilled in the art could not determine the boundaries of the claimed invention in order to avoid infringing on the claim.
Claim 41 recites “S444” and “S444C” but the claims fail to provide any frame of reference that would allow one of skill in the art to unambiguously identify the positions being referred to in the IgG. Accordingly, one skilled in the art could not determine the boundaries of the claimed invention in order to avoid infringing on the claim.
Note, amending claims 21 and 41 to recite “wherein the numbering is according to EU as set forth in Kabat” would obviate this rejection. See specification, para. [0122]. Please see para. [0122] in the specification as filed.
Claims 24 and 28 are included in the rejection because they are dependent on rejected claim and do not correct the deficiency of the claim from which they depend.
Applicants’ arguments filed January 30, 2026 have been fully considered but are not found persuasive.
Applicants’ position is that Without acquiescing to the propriety of any aspect of the rejections, claims 22-23, 25-27, 29-40 have been cancelled, thus obviating any rejection.
The MPEP holds that claim terms must be interpreted in view of the specification, and that explicit definitions in the specification control claim interpretation. See MPEP §2111.01 ("[t]he specification may define claim terms... such definitions are controlling."). As such, when the instant claims are read in light of the specification, a person of ordinary skill in the art would unambiguously understand that all recited residue positions (e.g., S444, S444C, F405L, K409R, and positions 405 and 409) refer to EU numbering as set forth in Kabat. Moreover, indefiniteness arises only when claim scope is not reasonably certain when read in light of the specification and the knowledge of one of ordinary skill in the art. See MPEP §2173.02. Here, the explicit designation of numbering convention removes any ambiguity and provides a clear reference for identifying the claimed amino acid positions. Accordingly, the claims particularly point out and distinctly claim the subject matter regarded as the invention.
Accordingly, it is respectfully requested that the 112(b) rejections of claims 21-40 be withdrawn.
In response, MPEP 2173.05(s) states that where possible, claims are to be complete inthemselves. A claim should not depend on tables or figures found in the specification for completeness but instead, should be able to stand alone.
MPEP 2173.02 states that "if the language of a claim, given its broadest reasonable interpretation, is such that a person of ordinary skill in the relevant art would read it with more than one reasonable interpretation, [a] rejection under 35 U.S.C. 112(b) or pre-AIA 35 U.S.C. 112, second paragraph is appropriate.” Further, MPEP 2173.02 II states that “If the language of the claim is such that a person of ordinary skill in the art could not interpret the metes and bounds of the claim so as to understand how to avoid infringement, a rejection of the claim under 35 U.S.C. 112(b) or pre-AIA 35 U.S.C. 112, second paragraph, is appropriate.
In this case, the claims are indefinite because, claim 21 recites S444, S444C, F405L, K409R but the claims fail to provide any frame of reference that would allow one of skill in the art to unambiguously identify the positions being referred to in the Fc region of an antibody. Claim 41 has a similar issue. Antibody amino acid sequences are not numbered consistently in the art and can be numbered by linear position or using art recognized antibody numbering indexes, for example, Dondelinger et al (Frontiers in Immunology 9(2278): 1-15, 2018; PTO 892) teaches that position can vary depending on the antibody and the numbering system used, e.g., Sequence-based numbering schemes, such as Kabat, EU and IMGT, structure-based numbering schemes such as Chothia, Martin, Gelfand, AbM, AHo. Accordingly, the metes and bounds of the claimed positions cannot be unambiguously construed.
For all of the above reasons it is submitted that the claims cannot be unambiguously construed and therefore fail to delineate the metes and bounds of the subject matter that is regarded as the invention with the requisite clarity and particularity to permit the skilled artisan to know or determine infringing subject matter, so as to satisfy the requirements set forth under 35 U.S.C. § 112, second paragraph.
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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form 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 http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 21, 24, 28 and 41 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 12,121,587. Although the conflicting claims are not identical, they are not patentably distinct from each other because the claims differ only in scope.
Issued claim 1 recites a dimeric immunotherapeutic, comprising a first chimeric immunotherapeutic and a second chimeric immunotherapeutic, wherein: the first chimeric immunotherapeutic comprises a first chimeric IgG that comprises a first light chain, a first heavy chain, a second light chain, and a second heavy chain, which each have an amino acid sequence numbered according to the EU numbering system; the second chimeric immunotherapeutic comprises a second chimeric IgG that comprises a first light chain, a first heavy chain, a second light chain, and a second heavy chain, which each have an amino acid sequence numbered according to the EU numbering system; the amino acid sequences of the first light chain of the first chimeric IgG and the first light chain of the second chimeric IgG are identical; the amino acid sequences of the second light chain of the first chimeric IgG and the second light chain of the second chimeric IgG are identical; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG are identical; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG are identical; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a mutation of a native amino acid to a cysteine; the cysteine of the amino acid sequence of the first heavy chain of the first chimeric IgG and the cysteine of the amino acid sequence of the first heavy chain of the second chimeric IgG form a disulfide bond with each other; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each lack the mutation; the first chimeric immunotherapeutic is chimeric at least because the amino acid sequence of the first heavy chain of the first chimeric IgG comprises the mutation and the amino acid sequence of the second heavy chain of the first chimeric IgG lacks the mutation such that the first chimeric IgG comprises two different heavy chains; the second chimeric immunotherapeutic is chimeric at least because the amino acid sequence of the first heavy chain of the second chimeric IgG comprises the mutation and the amino acid sequence of the second heavy chain of the second chimeric IgG lacks the mutation such that the second chimeric IgG comprises two different heavy chains; the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; the mutation is S444C; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R mutation; the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a heavy chain variable region that has an identical amino acid sequence; and the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a light chain variable region that has an identical amino acid sequence, which corresponds to instant claim 21.
Issued claim 2 recites a dimeric immunotherapeutic, comprising a first chimeric immunotherapeutic and a second chimeric immunotherapeutic, wherein: the first chimeric immunotherapeutic comprises a first chimeric IgG that comprises a first light chain, a first heavy chain, a second light chain, and a second heavy chain, which each have an amino acid sequence numbered according to the EU numbering system; the second chimeric immunotherapeutic comprises a second chimeric IgG that comprises a first light chain, a first heavy chain, a second light chain, and a second heavy chain, which each have an amino acid sequence numbered according to the EU numbering system; the amino acid sequences of the first light chain of the first chimeric IgG and the first light chain of the second chimeric IgG are identical; the amino acid sequences of the second light chain of the first chimeric IgG and the second light chain of the second chimeric IgG are identical; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG are identical; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG are identical; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a mutation of a native amino acid to a cysteine; the cysteine of the amino acid sequence of the first heavy chain of the first chimeric IgG and the cysteine of the amino acid sequence of the first heavy chain of the second chimeric IgG form a disulfide bond with each other; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each lack the mutation; the first chimeric immunotherapeutic is chimeric at least because the amino acid sequence of the first heavy chain of the first chimeric IgG comprises the mutation and the amino acid sequence of the second heavy chain of the first chimeric IgG lacks the mutation such that the first chimeric IgG comprises two different heavy chains; and the second chimeric immunotherapeutic is chimeric at least because the amino acid sequence of the first heavy chain of the second chimeric IgG comprises the mutation and the amino acid sequence of the second heavy chain of the second chimeric IgG lacks the mutation such that the second chimeric IgG comprises two different heavy chains, which corresponds to part of claim 21.
Issued claim 3 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; the mutation is S444C; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation; the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R mutation; the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a heavy chain variable region that has an identical amino acid sequence; and the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a light chain variable region that has an identical amino acid sequence, which corresponds to part of instant claim 21.
Issued claim 4 recites the dimeric immunotherapeutic of claim 2, wherein: the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a VH CDR1 region comprising an amino acid sequence that is identical to SEQ ID NO: 5; the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a VH CDR2 region comprising an amino acid sequence that is identical to SEQ ID NO: 6; the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a VH CDR3 region comprising an amino acid sequence that is identical to SEQ ID NO: 7; the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a VL CDR1 region comprising an amino acid sequence that is identical to SEQ ID NO: 8; the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a VL CDR2 region comprising an amino acid sequence that is identical to SEQ ID NO: 9; and the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a VL CDR3 region comprising an amino acid sequence that is identical to SEQ ID NO: 10, which corresponds to instant claim 24.
Issued claim 5 recites the dimeric immunotherapeutic of claim 2, wherein: the amino acid sequence of the first light chain of the first chimeric IgG is identical to SEQ ID NO: 4; the amino acid sequence of the first light chain of the second chimeric IgG is identical to SEQ ID NO: 4; the amino acid sequence of the second light chain of the first chimeric IgG is identical to SEQ ID NO: 4; the amino acid sequence of the second light chain of the second chimeric IgG is identical to SEQ ID NO: 4; the amino acid sequence of the first heavy chain of the first chimeric IgG is identical to SEQ ID NO: 3; the amino acid sequence of the first heavy chain of the second chimeric IgG is identical to SEQ ID NO: 3; the amino acid sequence of the second heavy chain of the first chimeric IgG is identical to SEQ ID NO: 3; and the amino acid sequence of the second heavy chain of the second chimeric IgG is identical to SEQ ID NO: 3, which corresponds to instant claim 25 as the reference SEQ ID NO: 4 and SEQ ID NO: 3 are at least 100% identical to the claimed SEQ ID NO: 4 and SEQ ID NO: 3, respectively.
Issued claim 6 recites the dimeric immunotherapeutic of claim 2, wherein: the amino acid sequence of the first light chain of the first chimeric IgG comprises SEQ ID NO: 4; the amino acid sequence of the first light chain of the second chimeric IgG comprises SEQ ID NO: 4; the amino acid sequence of the second light chain of the first chimeric IgG comprises SEQ ID NO: 4; the amino acid sequence of the second light chain of the second chimeric IgG comprises SEQ ID NO: 4; the amino acid sequence of the first heavy chain of the first chimeric IgG comprises SEQ ID NO: 3; the amino acid sequence of the first heavy chain of the second chimeric IgG comprises SEQ ID NO: 3; the amino acid sequence of the second heavy chain of the first chimeric IgG comprises SEQ ID NO: 3; and the amino acid sequence of the second heavy chain of the second chimeric IgG comprises SEQ ID NO: 3, which corresponds to instant claim 25 as the reference SEQ ID NO: 4 and SEQ ID NO: 3 are at least 100% identical to the claimed SEQ ID NO: 4 and SEQ ID NO: 3, respectively.
Issued claim 7 recites the dimeric immunotherapeutic of claim 2, wherein: the amino acid sequences of the first light chain of the first chimeric immunotherapeutic, the second light chain of the first chimeric immunotherapeutic, the first light chain of the second chimeric immunotherapeutic, and the second light chain of the second chimeric immunotherapeutic are identical; and the amino acid sequences of the first heavy chain of the first chimeric immunotherapeutic, the second heavy chain of the first chimeric immunotherapeutic, the first heavy chain of the second chimeric immunotherapeutic, and the second heavy chain of the second chimeric immunotherapeutic each have at least 90 percent sequence identity.
Issued claim 8 recites the dimeric immunotherapeutic of claim 2, wherein the amino acid sequences of the first light chain of the first chimeric immunotherapeutic, the second light chain of the first chimeric immunotherapeutic, the first light chain of the second chimeric immunotherapeutic, and the second light chain of the second chimeric immunotherapeutic are identical.
Issued claim 9 recites the dimeric immunotherapeutic of claim 2, wherein the amino acid sequences of the first heavy chain of the first chimeric immunotherapeutic, the second heavy chain of the first chimeric immunotherapeutic, the first heavy chain of the second chimeric immunotherapeutic, and the second heavy chain of the second chimeric immunotherapeutic each have at least 90 percent sequence identity.
Issued claim 10 recites the dimeric immunotherapeutic of claim 2, wherein: the first heavy chain of the first chimeric IgG, the second heavy chain of the first chimeric IgG, the first heavy chain of the second chimeric IgG, and the second heavy chain of the second chimeric IgG each comprise a heavy chain variable region that has an identical amino acid sequence; and the first light chain of the first chimeric IgG, the second light chain of the first chimeric IgG, the first light chain of the second chimeric IgG, and the second light chain of the second chimeric IgG each comprise a light chain variable region that has an identical amino acid sequence.
Issued claim 11 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG4s; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include an arginine at amino acid position 409 and a leucine at amino acid position 405; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a lysine at amino acid position 409 and a phenylalanine at amino acid position 405, which corresponds to part of instant claim 41.
Issued claim 12 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG4s; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a lysine at amino acid position 409 and a phenylalanine at amino acid position 405; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include an arginine at amino acid position 409 and a leucine at amino acid position 405, which corresponds to instant claim 41.
Issued claim 13 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; the mutation is S444C; the amino acid sequences of the first light chain of the first chimeric immunotherapeutic, the second light chain of the first chimeric immunotherapeutic, the first light chain of the second chimeric immunotherapeutic, and the second light chain of the second chimeric immunotherapeutic are identical; and the amino acid sequences of the first heavy chain of the first chimeric immunotherapeutic, the second heavy chain of the first chimeric immunotherapeutic, the first heavy chain of the second chimeric immunotherapeutic, and the second heavy chain of the second chimeric immunotherapeutic each have at least 90 percent sequence identity.
Issued claim 14 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; the mutation is S444C; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R mutation, which corresponds to instant claim 21.
Issued claim 15 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; the mutation is S444C; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a K409R mutation; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a F405L mutation, which corresponds to instant claim 21.
Issued claim 16 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R mutation, which corresponds to instant claim 21.
Issued claim 17 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a K409R mutation; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a F405L mutation, which corresponds to instant claim 21.
Issued claim 18 recites the dimeric immunotherapeutic of claim 2, wherein: the first chimeric IgG and the second chimeric IgG are both chimeric human IgG1s; the native amino acid is S444; and the mutation is S444C, which corresponds to instant claim 21.
Issued claim 19 recites the dimeric immunotherapeutic of claim 2, wherein: the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include an arginine at amino acid position 409 and a leucine at amino acid position 405; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a lysine at amino acid position 409 and a phenylalanine at amino acid position 405, which corresponds to instant claim 21.
Issued claim 20 recites the dimeric immunotherapeutic of claim 2, wherein: the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a lysine at amino acid position 409 and a phenylalanine at amino acid position 405; and the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include an arginine at amino acid position 409 and a leucine at amino acid position 405, which corresponds to instant claim 21.
Otherwise claims 21, 24, 28 and 41 are anticipated by the issued claims.
Applicants’ arguments filed January 30, 2026 have been fully considered but are not found persuasive.
Applicants’ position is that claims 22-23, 25-27, 29-40 are cancelled, thus obviating any rejection. Claim 21 has been amended to recite
"...the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L or a K409R mutation;
the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R or a F405L mutation;
Claims 24 and 28 are further amended to depend from claim 21.
In response, the term “or” does not require “…the first heavy chain of the second chimeric IgG each include a K409R mutation and …the second heavy chain of the second chimeric IgG does not include F405L mutation…”.
Claim 1 of the ‘587 patent recites “…the amino acid sequence of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R…”.
Regarding instant claim 24, the issued claim 4 recites the claimed VH and VL CDRs.
19/002,112
12,121,587
SEQ ID NO: 5
GGTFSSYAIS
GGTFSSYAIS
SEQ ID NO: 6
RIIPILGIANYAQKFQG
RIIPILGIANYAQKFQG
SEQ ID NO: 7
ARPSEEVVAAYGAFDI
ARPSEEVVAAYGAFDI
SEQ ID NO: 8
RASQSLLRSDGFNYLD
RASQSLLRSDGFNYLD
SEQ ID NO: 9
LGSNRAS
LGSNRAS
SEQ ID NO: 10
MQAVQTPYIF
MQAVQTPYIF
Regarding instant claim 28, issued claim 7 corresponds to instant claim 28. For these reasons, the rejection is maintained.
Claims 21, 24, 28 and 41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of US Patent 12,116,410 (reference).
Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims recite the same dimeric immunotherapeutic produced by the methods in claims 1-20 of US Patent 12,116,410.
The reference claims recite the method of producing dimeric immunotherapeutic comprising the same amino acid substitution of S444C in the HC of the first IgG, as well as for position 405 and 409 amino acids for both IgG1 and IgG4 molecules. The amino acids sequences of the CDRs, VL, and VH for the same anti-Sp17 antibody are recited in claims 4, 5 and 6 of the reference and the instant claims 24-26.
Applicants’ arguments filed January 30, 2026 have been fully considered but are not found persuasive.
Applicants’ position is that claims 22-23, 25-27, 29-40 are cancelled, thus obviating any rejection. Claim 21 has been amended to recite
"...the amino acid sequences of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L or a K409R mutation;
the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R or a F405L mutation.
In response, the term “or” does not require “…the first heavy chain of the second chimeric IgG each include a K409R mutation and …the second heavy chain of the second chimeric IgG does not include F405L mutation…”.
Claim 1 of the ‘410 patent recites “…the amino acid sequence of the first heavy chain of the first chimeric IgG and the first heavy chain of the second chimeric IgG each include a F405L mutation the amino acid sequences of the second heavy chain of the first chimeric IgG and the second heavy chain of the second chimeric IgG each include a K409R…”.
Regarding instant claim 24, the issued claim 4 recites the claimed VH and VL CDRs.
19/002,112
12,116,410
SEQ ID NO: 5
GGTFSSYAIS
GGTFSSYAIS
SEQ ID NO: 6
RIIPILGIANYAQKFQG
RIIPILGIANYAQKFQG
SEQ ID NO: 7
ARPSEEVVAAYGAFDI
ARPSEEVVAAYGAFDI
SEQ ID NO: 8
RASQSLLRSDGFNYLD
RASQSLLRSDGFNYLD
SEQ ID NO: 9
LGSNRAS
LGSNRAS
SEQ ID NO: 10
MQAVQTPYIF
MQAVQTPYIF
For these reasons, the rejection is maintained.
Conclusion
No claim is allowed.
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 PHUONG HUYNH whose telephone number is (571)272-0846. The examiner can normally be reached on 9:00 a.m. to 6:30 p.m. The examiner can also be reached on alternate alternative Friday from 9:00 a.m. to 5:30 p.m.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Misook Yu, can be reached at 571-270-3497. The fax phone number for the organization where this application or proceeding is assigned is 571-272-0839.
Information regarding the status of an application may be obtained from Patent Center. Status information for published applications may be obtained from Patent Center. Status information for unpublished applications is available through Patent Center for authorized users only. Should you have questions about access to Patent Center, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) Form at https://www.uspto.gov/patents/uspto-automated- interview-request-air-form.
/PHUONG HUYNH/ Primary Examiner, Art Unit 1641