+++++++++++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 .
1. Claims 15 and 93-128 as amended on 01/05/2024 are pending and under consideration.
Specification
2. The disclosure is objected to because of the following informalities: The current application was filed after July 1, 2022, thus the WIPO Standard ST.26, Sequence Listing in XML format, applies to sequence disclosures. See 37 CFR § 1.831. An ST.26 Sequence Listing in XML must not include any sequences having fewer than 10 specifically defined nucleotides, or fewer than 4 specifically defined amino acids. See 37 CFR § 1.831(j).
The Sequence Listing Table on pp. 167-173 amino acid contains sequences of three amino acids in length, SEQ ID NOs: 14 and 32, and polynucleotides of 9 nucleotides, SEQ ID NOs: 13 and 31. These sequences are replaced with “000” in the Sequence Listing in XML because the sequences are less than 4 amino acid sequences or fewer than 10 specifically defined nucleotides. The SEQ ID NOs: 13, 14, 31 and 32 in the specification associated with these sequences in the specification should be deleted because the Sequence Listing in XML does not contain the short sequences.
Appropriate correction is required.
Claim Objections
3. Claim 106 is objected to because of the following informalities: Claim 106 contains sequences of three amino acids in length in SEQ ID NOs: 14 and 32. These sequences are replaced with “000” in the Sequence Listing in XML because the sequences are less than 4 amino acid sequences in length. See 37 CFR § 1.831(j). SEQ ID NOs: 14 and 32 in claim 106 should be deleted and replaced with the appropriate three amino acid sequence. For example, in claim 106 (a) delete SEQ ID NO: 14 and insert GAS.
Appropriate correction is required.
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.
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3. Claim 15, 93-101, 106-114, 119, 120, 122-124, 126 and 127 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-62 of U.S. Patent No. 11,866,502 (Daly et al. Jan. 9, 2024, IDS).
The ‘502 claims are drawn to:
1. An isolated monoclonal antibody or antigen-binding fragment thereof that binds to FGFR2, wherein the antibody or antigen-binding fragment thereof comprises three heavy chain CDRs (HCDR1, HCDR2, and HCDR3) contained within the heavy chain variable region (HCVR) amino acid sequence of SEQ ID NO: 2 or SEQ ID NO: 22, and three light chain CDRs (LCDR1, LCDR2, and LCDR3) contained within the light chain variable region (LCVR) amino acid sequence of SEQ ID NO: 10 or SEQ ID NO: 28.
2. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein the antibody or antigen-binding fragment thereof is fully human.
3. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein HCDR1 comprises the amino acid sequence of SEQ ID NO: 4; HCDR2 comprises the amino acid sequence of SEQ ID NO: 6; HCDR3 comprises the amino acid sequence of SEQ ID NO: 8; LCDR1 comprises the amino acid sequence of SEQ ID NO: 12; LCDR2 comprises the amino acid sequence of SEQ ID NO: 14; and LCDR3 comprises the amino acid sequence of SEQ ID NO: 16.
4. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein the anti-FGFR2 antibody or antigen-binding fragment thereof comprises an HCVR comprising the amino acid sequence of SEQ ID NO: 2 or an amino acid sequence that is at least 95% identical thereto; and an LCVR comprising the amino acid sequence of SEQ ID NO: 10 or an amino acid sequence that is at least 95% identical thereto.
5. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein the anti-FGFR2 antibody or antigen-binding fragment thereof comprises an HCVR comprising the amino acid sequence of SEQ ID NO: 2; and an LCVR comprising the amino acid sequence of SEQ ID NO: 10.
6. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein HCDR1 comprises the amino acid sequence of SEQ ID NO: 24; HCDR2 comprises the amino acid sequence of SEQ ID NO: 6; HCDR3 comprises the amino acid sequence of SEQ ID NO: 26; LCDR1 comprises the amino acid sequence of SEQ ID NO: 30; LCDR2 comprises the amino acid sequence of SEQ ID NO: 32; and LCDR3 comprises the amino acid sequence of SEQ ID NO: 34.
7. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein the anti-FGFR2 antibody or antigen-binding fragment thereof comprises an HCVR comprising the amino acid sequence of SEQ ID NO: 22 or an amino acid sequence that is at least 95% identical thereto; and an LCVR comprising the amino acid sequence of SEQ ID NO: 28 or an amino acid sequence that is at least 95% identical thereto.
8. The anti-FGFR2 antibody or antigen-binding fragment thereof of claim 1, wherein the anti-FGFR2 antibody or antigen-binding fragment thereof comprises an HCVR comprising the amino acid sequence of SEQ ID NO: 22; and an LCVR comprising the amino acid sequence of SEQ ID NO: 28.
9. A pharmaceutical composition comprising a therapeutically effective amount of the antibody or antigen-binding fragment thereof of claim 1 together with one or more pharmaceutically acceptable excipients.
10. A nucleic acid molecule encoding the antibody or antigen-binding fragment thereof of claim 1.
11. An expression vector comprising the nucleic acid molecule of claim 10.
12. A host cell containing the expression vector of claim 11.
Although the claims at issue are not identical, they are not patentably distinct from each other because the sequences SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 22, 24, 26, and 28 of the ‘502 claims are the same sequences as the instantly claimed SEQ ID NOs. See Sequence Listing-columns 255-262. Additionally, it is noted that the courts have found that the disclosure of the polypeptide makes the nucleic acid encoding the protein obvious as the methods of obtaining the nucleic acids are routine in the art and can be obtained with a reasonable expectation of success. See MPEP 2143(E)(Example 3), Ex parte Kubin, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007), and In re Kubin 90 USPQ2d 1417 (U. S. Court of Appeals Fed. Cir. 2009). Thus, the antibodies comprising SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 22, 24, 26, and 28 of the ‘502 claims, and nucleic acids and host cells make the claimed nucleic acids encoding the anti-FGFR2 human monoclonal antibody or antigen binding fragment thereof obvious.
4. Claims 125 and 128 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-65 of U.S. Patent No. 11,866,502 (Daly et al. Jan. 9, 2024, IDS) as applied to claims 15, 93-101, 106-114, 119, 120, 122-124, 126 and 127 above in further view of Sambrook et al. (Molecular Cloning A laboratory Manual, 2nd edition, Cold Spring Harbor, N.Y. 1989, pp. 16.3-36), “Sambrook”.
The ‘502 claims teach as set forth above, but do not teach a method of producing the anti-FGFR2 antibody or antigen binding fragment thereof.
Sambrook teaches that cloned genes are conventionally expressed using expression vectors and that expression of cloned proteins have been used to: (1) confirm the identity of a cloned gene by using immunological or functional assays to detect the encoded protein; (2) produce large amounts of proteins of biological interest that are normally available in only limited quantities from natural sources; (3) to study the biosynthesis and intracellular transport of proteins following their expression in various cell types; and (4) to elucidate structure-function relationships by analyzing the properties of normal and mutant proteins (para bridging pages 16.3 and 16.4).
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘502 claims and Sambrook to isolate the nucleic acid encoding the anti-FGFR2 antibody or antigen binding fragment thereof and clone the nucleic acids into an expression vector as taught by Sambrook for production of the antibody because Sambrook specifically teaches that expressed cloned proteins are used to: (1) confirm the identity of a cloned gene by using immunological or functional assays to detect the encoded protein; (2) produce large amounts of proteins of biological interest that are normally available in only limited quantities from natural sources; (3) to study the biosynthesis and intracellular transport of proteins following their expression in various cell types; and (4) to elucidate structure-function relationships by analyzing the properties of normal and mutant proteins. Thus, one would have been motivated to isolate the nucleic acid encoding the anti-FGFR2 antibody or antigen binding fragment thereof of the of the ‘502 claims for the production, characterization and use as taught by Sambrook and for the methods of treatment of the ‘502 claims.
Related Prior Art
5. Felgenhauer et al. (Nucleic Acids Res. 1990 18(16): 4927) teach a light chain variable region of a human monoclonal antibody to HIV-1 gp41 that comprises LCDR1 and 2 of SEQ ID NOs: 46 and 32 and the first 7 amino acids of LCDR3 of SEQ ID NO: 34. See Fig. 1 and Appendix. However, Felgenhauer does not teach or suggest the anti-FGFR2 antibody or antigen binding fragment thereof nucleic acid molecules as claimed.
Conclusion
6. Claims 15, 93-101, 106-114, 119, 120, and 122-128 are rejected. Claims 102-105, 115-118 and 121 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.
No claims allowed.
7. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Janet L Epps-Smith can be reached at 571-272-0757. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PETER J REDDIG/ Primary Examiner, Art Unit 1646
APPENDIX
Alignment of SEQ ID NOs: 46, 32, and 34 with the LCVR of Felgenhauer
Ig kappa chain V region - human (fragment)
C;Species: Homo sapiens (man)
C;Date: 21-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 21-Jan-2000
C;Accession: S11240
R;Felgenhauer, M.; Kohl, J.; Rueker, F.
Nucleic Acids Res. 18, 4927, 1990
A;Title: Nucleotide sequences of the cDNAs encoding the V-regions of H- and L-chains of a human monoclonal antibody specific to HIV-1 - gp41.
A;Reference number: S11239; MUID:90370490; PMID:1697678
A;Accession: S11240
A;Status: preliminary
A;Molecule type: mRNA
A;Residues: 1-127 <FEL>
A;Cross-references: UNIPARC:UPI0000113780; EMBL:X53612; NID:g23868; PIDN:CAA37674.1; PID:g762937
C;Superfamily: immunoglobulin V region; immunoglobulin homology
C;Keywords: heterotetramer; immunoglobulin
F;38-112/Domain: immunoglobulin homology <IMM>
Query Match 61.1%; Score 58.7; Length 127;
Best Local Similarity 23.2%;
Matches 16; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 QSISRW-----------------KAS---------------------------------- 9
|||||| |||
Db 49 QSISRWLAWYQQKPGKVPKLLIYKASSLESGVPSRFSGSGSGTEFTLTISSLQPDDFATY 108
Qy 10 --QQYNSYS 16
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Db 109 YCQQYNSYS 117