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 .
2. Applicant’s response filed on 11/17/2025 is acknowledged. The restriction requirement mailed on 09/23/2025 is withdrawn in view of Applicant’s amendments.
3. Newly added claims 53-82 are pending and under consideration for their full scope.
4. 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.
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5. Claims 53-82 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-26 of U.S. Patent No.12,030,945 (PTO-892; Reference A). Although the claims at issue are not identical, they are not patentably distinct from each other because:
Instant claims 53-82 are directed to a fusion protein comprising an Fc polypeptide linked to a heterologous protein, wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 88, provided that the Fc polypeptide comprises: a glutamic acid residue at position 237 and a glutamic acid residue at position 238, wherein the positions are according to EU numbering; an aspartic acid residue at position 237, a glycine residue at position 238, an alanine residue at position 240, an aspartic acid residue at position 269, a glutamic acid residue at position 270, and an arginine residue at position 330, wherein the positions are according to EU numbering; or a phenylalanine residue at position 234, a glutamic acid residue at position 235, an aspartic acid residue at position 268, a glycine residue at position 271, and an alanine residue at position 329, wherein the positions are according to EU numbering; wherein the Fc polypeptide having at least 95% identity to the amino acid sequence of SEQ ID NO: 88 comprises the glutamic acid residue at position 237 and the glutamic acid residue at position 238, wherein the positions are according to EU numbering; wherein the Fc polypeptide having at least 95% identity to the amino acid sequence of SEQ ID NO: 88 comprises the aspartic acid residue at position 237, the glycine residue at position 238, the alanine residue at position 240, the aspartic acid residue at position 269, the glutamic acid residue at position 270, and the arginine residue at position 330, wherein the positions are according to EU numbering; wherein the Fc polypeptide having at least 95% identity to the amino acid sequence of SEQ ID NO: 88 comprises the phenylalanine residue at Page 2 of 7 position 234, the glutamic acid residue at position 235, the aspartic acid residue at position 268, the glycine residue at position 271, and the alanine residue at position 329, wherein the positions are according to EU numbering; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 40; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 40; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 102; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 102; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 86; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 86; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 103; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 103; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 77; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 77; wherein the Fc polypeptide comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 104; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 104; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; wherein the heterologous protein is an antibody, or an antigen binding fragment thereof; a pharmaceutical composition comprising the fusion protein of claim 53 and a pharmaceutically acceptable excipient; wherein the Fc polypeptide is directly linked to the heterologous protein; and wherein the Fc polypeptide is linked to the heterologous protein with a peptide linker.
Claims 1-26 of U.S. Patent 12,030,945 are directed to an Fc polypeptide having at least 95% identity to an amino acid sequence comprising the amino acid sequence of SEQ ID NO: 88 provided that the Fc polypeptide comprises: a glutamic acid residue at position 237 and a glutamic acid residue at position 238, wherein the positions are according to EU numbering; an aspartic acid residue at position 237, a glycine residue at position 238, an alanine residue at position 240, an aspartic acid residue at position 269, a glutamic acid residue at position 270, and an arginine residue at position 330, wherein the positions are according to EU numbering; or a phenylalanine residue at position 234, a glutamic acid residue at position 235, an aspartic acid residue at position 268, a glycine residue at position 271, and an alanine residue at position 329, wherein the positions are according to EU numbering of claim 1; an Fc polypeptide having at least 95% identity to an amino acid sequence comprising the amino acid sequence of SEQ ID NO: 88 provided that the Fc polypeptide comprises a glutamic acid residue at position 237 and a glutamic acid residue at position 238, wherein the positions are according to EU numbering of claim 2; an Fc polypeptide having at least 95% identity to an amino acid sequence comprising the amino acid sequence of SEQ ID NO: 88 provided that the Fc polypeptide comprises an aspartic acid residue at position 237, a glycine residue at position 238, an alanine residue at position 240, an aspartic acid residue at position 269, a glutamic acid residue at position 270, and an arginine residue at position 330, wherein the positions are according to EU numbering of claim 3; an Fc polypeptide having at least 95% identity to an amino acid sequence comprising the amino acid sequence of SEQ ID NO: 88 provided that the Fc polypeptide comprises a phenylalanine residue at position 234, a glutamic acid residue at position 235, an aspartic acid residue at position 268, a glycine residue at position 271, and an alanine residue at position 329, wherein the positions are according to EU numbering of claim 4; wherein the Fc polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 40 of claim 5; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 40 of claim 6; wherein the Fc polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 102 of claim 7; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 102 of claim 8; wherein the Fc polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 86 of claim 9; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 86 of claim 10; wherein the Fc polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 103 of claim 11; the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 103 of claim 12; wherein the Fc polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 77 of claim 13; wherein the Fc polypeptide comprises the amino acid sequence of SEQ ID NO: 77 of claim 14; wherein the Fe polypeptide has at least 95% identity to an amino acid sequence comprising the sequence of SEQ ID NO: 104 of claim 15; wherein the Fe polypeptide comprises the amino acid sequence of SEQ ID NO: 104 of claim 16; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 1 of claim 17; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 5 of claim 18; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 6 of claim 19; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 8 of claim 20; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 10 of claim 21; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 12 of claim 22; a composition comprising a homodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide and the second polypeptide each comprise the Fc polypeptide of claim 14 of claim 23; a composition comprising a heterodimer comprising a first polypeptide and a second polypeptide, wherein the first polypeptide comprises the Fc polypeptide of claim 1 and the second polypeptide is not the same as the first polypeptide of claim 24; wherein the Fc polypeptide is linked to an inhibitory receptor effector domain of claim 25; wherein the inhibitory receptor effector domain is an antibody that binds to PD-1, LAG-3, or CTLA4 of claim 26; wherein the antibody is an antibody that binds to PD-1 of claim 27; wherein the antibody that binds to PD-1 is a PD-1 agonist of claim 28; a pharmaceutical composition comprising the Fc polypeptide of claim 1 of claim 29; and a pharmaceutical composition comprising the Fc polypeptide of claim 8 of claim 30.
The reference teachings anticipate the claimed invention.
Claim 82 in included in this rejection because the first portion of the second polypeptide of claim 24 or inhibitory receptor effector domain of claim 25 or antibody of claims 26-28 can be thought of as the “peptide linker” of instant claim 82. Alternatively, it would be obvious to have used a peptide linker when linking a Fc polypeptide to a polypeptide inhibitory receptor effector domain of claim 25 or antibody of claims 26-28, especially since the term “linked” was used in claim 25 of U.S. Patent 12,030,945 to describe the heterodimer.
From the combined teachings of the reference, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the reference, especially in the absence of evidence to the contrary.
6. No claim is allowed.
7. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (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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Janurary 10, 2026
/Nora M Rooney/
Primary Examiner, Art Unit 1641