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 29-36 are pending and being examined.
Priority
2. The instant application claims priority benefit to:
17/568,376 filed 01/04/2022 now US PAT 11964024;
PRO 63/172,968 filed 04/09/2021; and
PRO 63/133,707 filed 01/04/2021.
A review of the above documents does not reveal support for a vector comprising the claimed nucleic acid molecule or set of nucleic acid molecules encoding the recited antibody amino acid sequences, and does not reveal support for a cell comprising the nucleic acid molecule(s) or a vector. There is no mention of a vector of any sort in any of the priority documents. There is no mention of a cell or host cell comprising the claimed nucleic acid molecules. There does not appear to be support for the material recited in instant claims 34-36. Therefore, claims 34-36 receive only the priority benefit of the instant application’s filing date March 5, 2024.
Specification
3. The disclosure is objected to because of the following informalities: The specification refers to SEQ ID NO:54 in numerous locations, such as p. 135, [519]; p. 39, [538]; p. 140, [540]; and p. 141, [540-545], however, SEQ ID NO:54 is identified as “000” in the sequence listing. The specification should be amended to identify “GAS” as the sequence wherever SEQ ID NO:54 is disclosed. Appropriate correction is required.
Claim Objections
4. Claim 29 is objected to because of the following informalities: claim 1 recites “GAS (SEQ ID NO:54), however SEQ ID NO:54 is identified as “000” in the sequence listing and no longer represents “GAS”. The phrase “(SEQ ID NO:54)” should be deleted from claim 29. Appropriate correction is required.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Section 33(a) of the America Invents Act reads as follows:
Notwithstanding any other provision of law, no patent may issue on a claim directed to or encompassing a human organism.
5. Claims 35 and 36 are rejected under 35 U.S.C. 101 and section 33(a) of the America Invents Act as being directed to or encompassing a human organism. See also Animals - Patentability, 1077 Off. Gaz. Pat. Office 24 (April 21, 1987) (indicating that human organisms are excluded from the scope of patentable subject matter under 35 U.S.C. 101). Claims 35 and 36 broadly encompass cells that can be found in a human organism, therefore are directed to or encompass humans.
Claim Rejections - 35 USC § 103
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.
6. Claim(s) 34-36 are rejected under 35 U.S.C. 103 as being unpatentable over US Patent Application Publication 2022/0233707, Lowinger et al, published July 2022; in view of WO 2007067991, Korman et al, published June 2007; and Li et al (mAbs, 2010, 2:5, 466-477).
Lowinger teaches nucleic acid molecule encoding an antibody that specifically binds B7-H4 and comprises the instantly claimed CDR SEQ ID NOs:2, 3, 10 or 16, 53, GAS, and 55; heavy and light chain variable SEQ ID NOs:44 and 50; heavy and light chain SEQ ID NOs:45 and 52; 22 and 50; or 23 and 52; heavy chain constant region SEQ ID NO:6; and light chain constant region 51 ([8-11]; [71]; [730]; [731-743]; [754]; Table 1; claims 1-3 and 10-11). Lowinger teaches the encoded antibody is intended for therapeutic administration or pharmaceutical use (claims 19, 25-29; [1086-1088]; [1102]). Lowinger teaches the antibodies are derived from parental anti-B7-H4 antibody 2F9 ([726-734]).
Lowinger does not teach a vector comprising the nucleic acid molecule, a cell comprising the nucleic acid molecule, or a cell comprising the vector.
Korman teaches parental anti-B7-H4 (anti-O8E) human antibody 2F9 that comprises light chain variable region SEQ ID NO:8 that is 100% identical to instant light chain variable region SEQ ID NO:50 and comprises 100% of instant CDR SEQ ID NOs:53, GAS, and 55; and comprises heavy chain variable region SEQ ID NO:3 that comprises instant CDR1 and CDR2 SEQ ID NOs:2 and 3, but comprises a CDR3 having one substitution mutation relative to instant SEQ ID NO:10 or comprises two substitution mutations relative to instant SEQ ID NO:16 (see sequence alignments below). Korman teaches nucleic acid molecules encoding the antibody, expression vectors comprising the nucleic acid molecules, and host cells comprising the expression vectors for producing the antibody for pharmaceutical use (p. 8, lines 23-30; p. 48-52; p. 54-56; p. 67-70).
Li reviews routine methods of producing therapeutic antibodies for pharmaceutical use, which comprises transfecting mammalian cells with a nucleic acid vector encoding the antibody and expressing the antibody for isolation and production of a pharmaceutical (abstract; p. 467-471; Table 1).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed to provide a vector comprising the nucleic acid molecule of Lowinger and a cell comprising the nucleic acid molecule or vector. One would have been motivated to, and have a reasonable expectation of success to, because: (1) Lowinger teaches utilizing their antibody for pharmaceutical administration; (2) Korman teaches the parental anti-B7-H4 antibody of Lowinger, and nucleic acids encoding it, vectors comprising the nucleic acid, and host cells comprising the vectors to express and produce the antibody for pharmaceutical use; (3) Li teaches antibodies intended for pharmaceutical administration are routinely expressed by and produced in mammalian cell culture that is transfected with vectors comprising a nucleic acid molecule encoding the antibody.
SEQ ID NO:50 light chain variable region:
RESULT 1
AGD58552
ID AGD58552 standard; protein; 109 AA.
XX
AC AGD58552;
XX
DT 09-AUG-2007 (first entry)
XX
DE Anti-O8E human monoclonal antibody 2F9 VL region.
XX
KW O8E; tumor marker; antibody therapy; monoclonal antibody;
KW immunoconjugate; breast tumor; ovary tumor; renal tumor;
KW head & neck tumor; neoplasm; cytostatic; 2F9;
KW light chain variable region.
XX
OS Homo sapiens.
XX
FH Key Location/Qualifiers
FT Region 24..35
FT /label= L-CDR1
FT Region 51..57
FT /label= L-CDR2
FT Region 90..99
FT /label= L-CDR3
XX
CC PN WO2007067991-A2.
XX
CC PD 14-JUN-2007.
XX
CC PF 08-DEC-2006; 2006WO-US061816.
XX
PR 08-DEC-2005; 2005US-0748914P.
PR 05-SEP-2006; 2006US-0824593P.
XX
CC PA (MEDA-) MEDAREX INC.
XX
CC PI Korman AJ, Selby MJ, Lu L, Witte A, Huang H;
XX
DR WPI; 2007-468955/45.
DR N-PSDB; AGD58592.
XX
CC PT New monoclonal antibody to O8E, useful for treating cancer, e.g. breast
CC PT cell carcinoma, ovarian cancer, kidney cancer, or head and neck cancer.
XX
CC PS Claim 13; SEQ ID NO 8; 151pp; English.
XX
CC The present invention provides isolated monoclonal antibodies (MAbs) that
CC exhibit high binding affinity to tumor marker O8E (also known as B7H4,
CC B7S1 and B7x) and which are useful for treating O8E mediated diseases,
CC especially cancer. Typically, the antibody is a human antibody, although
CC it may also be a murine antibody, a chimeric antibody or a humanized
CC antibody. It may also be an antibody fragment or a single chain antibody.
CC In certain embodiments, the antibody binds to a breast cell carcinoma
CC tumor cell line, such as SKBR3 (ATCC HTB-30). The antibody may be
CC internalized by SKBR3 tumor cells after binding to O8E expressed on those
CC cells. The invention also provides: immunoconjugates comprising an
CC antibody of the invention (or its antigen-binding portion) linked to a
CC therapeutic agent such as a cytotoxin or radioactive isotope; nucleic
CC acids encoding the antibodies of the invention, as well as vectors, host
CC cells and methods of making anti-O8E antibodies using such host cells;
CC and a method of treating or preventing a disease characterized by growth
CC of tumor cells expressing O8E by administering an anti-O8E antibody of
CC the invention, where the disease is cancer, in particular breast cell
CC carcinoma, ovarian cancer, kidney cancer and head and neck cancer. Human
CC MAbs of the invention are designated 1G11, 2A7, 2F9, 12E1 and 13D12.
CC These were obtained by immunizing human antibody gene-expressing
CC transgenic mice with O8E, and fusing splenocytes with mouse myeloma cells
CC to obtain hybridoma lines. The heavy chain variable region (VH) and light
CC chain variable region (VL) sequences of these MAbs, and the nucleotide
CC sequences encoding them, are provided. Preferred antibodies of the
CC invention include these VL and VH regions, or the complementarity
CC determining regions (CDRs) from them. The present sequence is that of the
CC MAb 2F9 VL region (V-segment A27; J-segment JK2).
XX
SQ Sequence 109 AA;
Query Match 100.0%; Score 562; DB 10; Length 109;
Best Local Similarity 100.0%;
Matches 109; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIP 60
Qy 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLYTFGQGTKLEIK 109
|||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLYTFGQGTKLEIK 109
SEQ ID NOs:2+3+10 heavy chain variable region CDRs:
RESULT 17
AGD58547
ID AGD58547 standard; protein; 116 AA.
XX
AC AGD58547;
XX
DT 09-AUG-2007 (first entry)
XX
DE Anti-O8E human monoclonal antibody 2F9 VH region.
XX
KW O8E; tumor marker; antibody therapy; monoclonal antibody;
KW immunoconjugate; breast tumor; ovary tumor; renal tumor;
KW head & neck tumor; neoplasm; cytostatic; 2F9;
KW heavy chain variable region.
XX
OS Homo sapiens.
XX
FH Key Location/Qualifiers
FT Region 31..35
FT /label= H-CDR1
FT Region 50..65
FT /label= H-CDR2
FT Region 98..105
FT /label= H-CDR3
XX
CC PN WO2007067991-A2.
XX
CC PD 14-JUN-2007.
XX
CC PF 08-DEC-2006; 2006WO-US061816.
XX
PR 08-DEC-2005; 2005US-0748914P.
PR 05-SEP-2006; 2006US-0824593P.
XX
CC PA (MEDA-) MEDAREX INC.
XX
CC PI Korman AJ, Selby MJ, Lu L, Witte A, Huang H;
XX
DR WPI; 2007-468955/45.
DR N-PSDB; AGD58587.
XX
CC PT New monoclonal antibody to O8E, useful for treating cancer, e.g. breast
CC PT cell carcinoma, ovarian cancer, kidney cancer, or head and neck cancer.
XX
CC PS Claim 13; SEQ ID NO 3; 151pp; English.
XX
CC The present invention provides isolated monoclonal antibodies (MAbs) that
CC exhibit high binding affinity to tumor marker O8E (also known as B7H4,
CC B7S1 and B7x) and which are useful for treating O8E mediated diseases,
CC especially cancer. Typically, the antibody is a human antibody, although
CC it may also be a murine antibody, a chimeric antibody or a humanized
CC antibody. It may also be an antibody fragment or a single chain antibody.
CC In certain embodiments, the antibody binds to a breast cell carcinoma
CC tumor cell line, such as SKBR3 (ATCC HTB-30). The antibody may be
CC internalized by SKBR3 tumor cells after binding to O8E expressed on those
CC cells. The invention also provides: immunoconjugates comprising an
CC antibody of the invention (or its antigen-binding portion) linked to a
CC therapeutic agent such as a cytotoxin or radioactive isotope; nucleic
CC acids encoding the antibodies of the invention, as well as vectors, host
CC cells and methods of making anti-O8E antibodies using such host cells;
CC and a method of treating or preventing a disease characterized by growth
CC of tumor cells expressing O8E by administering an anti-O8E antibody of
CC the invention, where the disease is cancer, in particular breast cell
CC carcinoma, ovarian cancer, kidney cancer and head and neck cancer. Human
CC MAbs of the invention are designated 1G11, 2A7, 2F9, 12E1 and 13D12.
CC These were obtained by immunizing human antibody gene-expressing
CC transgenic mice with O8E, and fusing splenocytes with mouse myeloma cells
CC to obtain hybridoma lines. The heavy chain variable region (VH) and light
CC chain variable region (VL) sequences of these MAbs, and the nucleotide
CC sequences encoding them, are provided. Preferred antibodies of the
CC invention include these VL and VH regions, or the complementarity
CC determining regions (CDRs) from them. The present sequence is that of the
CC MAb 2F9 VH region (V-segment VH3-53; D-segment D5-24; J-segment JH6b).
XX
SQ Sequence 116 AA;
Query Match 77.7%; Score 102.5; DB 10; Length 116;
Best Local Similarity 30.0%;
Matches 24; Conservative 0; Mismatches 1; Indels 55; Gaps 2;
Qy 1 GFIVSRNY-----------------IYGSGRT---------------------------- 15
|||||||| |||||||
Db 26 GFIVSRNYMNWVRQAPGKGLEWVSVIYGSGRTDCADSVKGRFTISRDNSKNTLYLQMNSL 85
Qy 16 ----------ARDADYGMDV 25
||| ||||||
Db 86 RAEDTAVYYCARDGDYGMDV 105
SEQ ID NOs:2+3+16 heavy chain variable region CDRs:
Query Match 76.0%; Score 99.5; Length 116;
Best Local Similarity 28.8%;
Matches 23; Conservative 1; Mismatches 1; Indels 55; Gaps 2;
Qy 1 GFIVSRNY-----------------IYGSGRT---------------------------- 15
|||||||| |||||||
Db 26 GFIVSRNYMNWVRQAPGKGLEWVSVIYGSGRTDCADSVKGRFTISRDNSKNTLYLQMNSL 85
Qy 16 ----------ARDADYGLDV 25
||| |||:||
Db 86 RAEDTAVYYCARDGDYGMDV 105
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.
7. Claims 29-36 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of U.S. Patent No. 11,964,024 in view of WO 2007067991, Korman et al, published June 2007; and Li et al (mAbs, 2010, 2:5, 466-477).
The US Patent claims:
1. An isolated antibody that specifically binds B7-H4 comprising a variable heavy chain complementarity determining region 1 (CDRH1) comprising the amino acid sequence GFIVSRNY (SEQ ID NO: 2), a variable heavy chain complementarity determining region 2 (CDRH2) comprising the amino acid sequence IYGSGRT (SEQ ID NO: 3), a variable heavy chain complementarity determining region 3 (CDRH3) comprising the amino acid sequence ARDADYGLDV (SEQ ID NO: 16) or the amino acid sequence ARDADYGMDV (SEQ ID NO: 10), a variable light chain complementarity determining region 1 (CDRL1) comprising the amino acid sequence QSVSSSY (SEQ ID NO: 53), a variable light chain complementarity determining region 2 (CDRL2) comprising the amino acid sequence GAS (SEQ ID NO: 54), and a variable light chain complementarity determining region 3 (CDRL3) comprising the amino acid sequence QQYGSSPLYT (SEQ ID NO: 55).
2. The isolated antibody of claim 1, wherein the isolated antibody comprises a heavy chain variable sequence comprising the amino acid sequence of SEQ ID NO: 44 and a light chain variable sequence comprising the amino acid sequence of SEQ ID NO: 50.
3. The isolated antibody of claim 1, wherein the isolated antibody comprises (i) a heavy chain comprising the amino acid sequence of SEQ ID NO: 45 and a light chain comprising the amino acid sequence of SEQ ID NO: 52; (ii) a heavy chain variable sequence comprising the amino acid sequence of SEQ ID NO: 22 and a light chain variable sequence comprising the amino acid sequence of SEQ ID NO: 50; or (iii) a heavy chain comprising the amino acid sequence of SEQ ID NO: 23 and a light chain comprising the amino acid sequence of SEQ ID NO: 52.
4. The isolated antibody of claim 1, wherein the isolated antibody is a monoclonal antibody.
5. The isolated antibody of claim 4, wherein the isolated antibody is a chimeric, humanized or fully human monoclonal antibody.
6. The isolated antibody of claim 1, wherein the isolated antibody is an IgG isotype or an IgG1 isotype antibody.
7. The isolated antibody of claim 1, wherein the isolated antibody competes for specific binding to human B7-H4 with an isolated antibody comprising a variable heavy chain complementarity determining region 1 (CDRH1) comprising the amino acid sequence GFIVSRNY (SEQ ID NO: 2), a variable heavy chain complementarity determining region 2 (CDRH2) comprising the amino acid sequence IYGSGRT (SEQ ID NO: 3), a variable heavy chain complementarity determining region 3 (CDRH3) comprising the amino acid sequence ARDADYGLDV (SEQ ID NO: 16) or the amino acid sequence ARDADYGMDV (SEQ ID NO: 10), a variable light chain complementarity determining region 1 (CDRL1) comprising the amino acid sequence QSVSSSY (SEQ ID NO: 53), a variable light chain complementarity determining region 2 (CDRL2) comprising the amino acid sequence GAS (SEQ ID NO: 54), and a variable light chain complementarity determining region 3 (CDRL3) comprising the amino acid sequence QQYGSSPLYT (SEQ ID NO: 55).
8. The isolated antibody of claim 1, wherein the isolated antibody competes for specific binding to human B7-H4 with an isolated antibody comprising a heavy chain variable sequence comprising the amino acid sequence of SEQ ID NO: 44 and a light chain variable sequence comprising the amino acid sequence of SEQ ID NO: 50 or with an isolated antibody comprising a heavy chain comprising the amino acid sequence of SEQ ID NO: 45 and a light chain comprising the amino acid sequence of SEQ ID NO: 52.
9. A B7-H4 antibody-drug conjugate comprising the isolated antibody of claim 1.
15. A method of treating a B7-H4 positive disease or disorder in a subject in need thereof, comprising administering to the subject a B7-H4 antibody-drug conjugate of claim 9.
16. The method of claim 15, wherein the B7-H4 positive disease or disorder is a B7-H4 positive cancer.
17. The method of claim 16, wherein the B7-H4 positive cancer is bile duct carcinoma, breast cancer, endometrial cancer, ovarian cancer, non-small cell lung cancer, small cell lung cancer, uterine cancer, thyroid cancer, kidney cancer, head and neck cancer, gastric cancer, melanoma, bile duct carcinoma, cholangial carcinoma, pancreatic cancer, colon cancer or bladder cancer.
18. The method of claim 17, wherein the B7-H4 positive cancer is breast cancer, endometrial cancer, ovarian cancer, or cholangial carcinoma.
19. The method of claim 15, further comprising administration of a therapeutic agent to the subject.
20. A pharmaceutical composition comprising the B7-H4 antibody-drug conjugate of claim 9 and a pharmaceutically acceptable carrier.
25. The isolated antibody of claim 1, wherein the isolated antibody comprises a heavy chain comprising a heavy chain variable sequence comprising the amino acid sequence of SEQ ID NO: 44 and a heavy chain constant region comprising the amino acid sequence of SEQ ID NO: 6; and
a light chain comprising a light chain variable sequence comprising the amino acid sequence of SEQ ID NO: 50 and a light chain constant region comprising the amino acid sequence of SEQ ID NO: 51.
26. The isolated antibody of claim 1, wherein the isolated antibody comprises a heavy chain comprising a heavy chain variable sequence comprising the amino acid sequence of SEQ ID NO: 22 and a heavy chain constant region comprising the amino acid sequence of SEQ ID NO: 6; and
a light chain comprising a light chain variable sequence comprising the amino acid sequence of SEQ ID NO: 50 and a light chain constant region comprising the amino acid sequence of SEQ ID NO: 51.
Therefore, the US Patent claims an anti-B7-H4 antibody comprising the same amino acid sequences as the antibody encoded by the instant nucleic acid molecules claimed.
The US Patent does not claim nucleic acid molecules encoding the claimed antibody amino acid sequences.
The US Patent does not claim a vector comprising the nucleic acid molecule encoding the antibody sequences, a cell comprising the nucleic acid molecule, or a cell comprising the vector.
Korman teaches parental anti-B7-H4 (anti-O8E) human antibody 2F9 that comprises light chain variable region SEQ ID NO:8 that is 100% identical to instant light chain variable region SEQ ID NO:50 and comprises 100% of instant CDR SEQ ID NOs:53, GAS, and 55; and comprises heavy chain variable region SEQ ID NO:3 that comprises instant CDR1 and CDR2 SEQ ID NOs:2 and 3, but comprises a CDR3 having one substitution mutation relative to instant SEQ ID NO:10 or comprises two substitution mutations relative to instant SEQ ID NO:16 (see sequence alignments below). Korman teaches nucleic acid molecules encoding the antibody, expression vectors comprising the nucleic acid molecules, and host cells comprising the expression vectors for producing the antibody for pharmaceutical use (p. 8, lines 23-30; p. 48-52; p. 54-56; p. 67-70).
Li reviews routine methods of producing therapeutic antibodies for pharmaceutical use, which comprises transfecting mammalian cells with a nucleic acid vector encoding the antibody and expressing the antibody for isolation and production of a pharmaceutical (abstract; p. 467-471; Table 1).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed to provide nucleic acid molecule encoding the antibody of the US Patent, a vector comprising the nucleic acid molecule encoding the antibody, and a cell comprising the nucleic acid molecule or vector. One would have been motivated to, and have a reasonable expectation of success to, because: (1) the US Patent claims utilizing their antibody for pharmaceutical administration; (2) Korman teaches the parental anti-B7-H4 antibody of the US Patent, and nucleic acids encoding it, vectors comprising the nucleic acid, and host cells comprising the vectors to express and produce the antibody for pharmaceutical use; and (3) Li teaches antibodies intended for pharmaceutical administration are routinely expressed by and produced in mammalian cell culture that is transfected with vectors comprising a nucleic acid molecule encoding the antibody.
8. Claims 29-36 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-27 of copending Application No. 18/319,176 in view of WO 2007067991, Korman et al, published June 2007; and Li et al (mAbs, 2010, 2:5, 466-477).
The copending application claims a method for treating cancer comprising administering to a subject anti-B7-H4 antibody comprising CDR sequences identical to instant SEQ ID NOs:2, 3, 16, 53, GAS, and 55 (copending SEQ ID NOs:2, 3, 4, 5, GAS, 7); instant heavy chain variable region SEQ ID NO:44 (copending SEQ ID NO:9); instant light chain variable region SEQ ID NO:50 (copending SEQ ID NO:8); instant heavy chain SEQ ID NO:45 and 6 (copending SEQ ID NO:13), and instant light chain SEQ ID NO:52 and 51 (copending SEQ ID NO:12). Therefore, the copending application obviates the B7-H4 antibody amino acid sequences encoded by the instantly claimed nucleic acid molecule.
The copending application does not claim nucleic acid molecules encoding the claimed antibody amino acid sequences.
The copending application does not claim a vector comprising the nucleic acid molecule encoding the antibody sequences, a cell comprising the nucleic acid molecule, or a cell comprising the vector.
Korman teaches parental anti-B7-H4 (anti-O8E) human antibody 2F9 that comprises light chain variable region SEQ ID NO:8 that is 100% identical to copending application light chain variable region SEQ ID NO:8 and comprises 100% of copending application CDR SEQ ID NOs:5, GAS, and 7; and comprises heavy chain variable region SEQ ID NO:3 that comprises instant CDR1 and CDR2 SEQ ID NOs:2 and 3, but comprises a CDR3 having one substitution mutation relative to the copending application CDR3 SEQ ID NO: 4. Korman teaches nucleic acid molecules encoding the antibody, expression vectors comprising the nucleic acid molecules, and host cells comprising the expression vectors for producing the antibody for pharmaceutical use (p. 8, lines 23-30; p. 48-52; p. 54-56; p. 67-70).
Li reviews routine methods of producing therapeutic antibodies for pharmaceutical use, which comprises transfecting mammalian cells with a nucleic acid vector encoding the antibody and expressing the antibody for isolation and production of a pharmaceutical (abstract; p. 467-471; Table 1).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed to provide nucleic acid molecule encoding the antibody of the copending application, a vector comprising the nucleic acid molecule encoding the antibody, and a cell comprising the nucleic acid molecule or vector. One would have been motivated to, and have a reasonable expectation of success to, because: (1) the copending application claims utilizing their antibody for pharmaceutical administration; (2) Korman teaches the parental anti-B7-H4 antibody of the copending application, and nucleic acids encoding it, vectors comprising the nucleic acid, and host cells comprising the vectors to express and produce the antibody for pharmaceutical use; and (3) Li teaches antibodies intended for pharmaceutical administration are routinely expressed by and produced in mammalian cell culture that is transfected with vectors comprising a nucleic acid molecule encoding the antibody.
This is a provisional nonstatutory double patenting rejection.
9. Conclusion: No claim is allowed.
10. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LAURA B GODDARD whose telephone number is (571)272-8788. The examiner can normally be reached Mon-Fri, 7am-3:30pm.
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/Laura B Goddard/Primary Examiner, Art Unit 1642
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