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 1-28 are pending and currently under consideration.
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.
Claim 11 is 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 the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 11 is rejected because it is unclear how, or if, test following the term “particularly” limits the claim. Therefore, the metes-and-bounds of the claim are unclear.
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.
Claim(s) 1-28 is/are rejected under 35 U.S.C. 103 as being unpatentable over Bacac et al WO 2019/086497 (priority to 11/1/2017) or Bacac et al US 20200392237 (priority to 11/1/2017) in view of [{Bruenker et al WO 2020/070041 (priority to 10/1/2018) or US 11242396 (priority to 10/1/2018) or US 20200190207 (priority to 10/1/2018)} or {Duerr et al WO 2020/070035 (priority to 10/1/2018) or US 20210292426 (priority to 10/1/2018)}] and Du et al WO 2015/153513.
The claims in the instant application are directed to bispecific molecules comprising at least two binding domains to OX40, a binding domain to FAP and Fc regions composed of a first and second subunit capable of stable association and treatment methods comprising administering the bispecific molecules. The sequences correspond to clones as follows:
Clone 49B4--OX40 binding domain comprising a VH containing CDRs of SEQ ID NO. 27,28 and 29 and a VL containing CDRs of SEQ ID NOL. 30, 31 and 32 .
Clone CLC563--OX40 binding domain comprising a VH containing CDRs of SEQ ID NO. 35, 36 and 37 and a VL containing CDRs of SEQ ID NOL. 38, 39 and 40.
Clone MOXR0916-- OX40 binding domain comprising a VH containing CDRs of SEQ ID NO. 43, 44 and 45 and a VL containing CDRs of SEQ ID NOL. 46, 47 and 48.
Clone 8H9-- OX40 binding domain comprises a VH containing CDRs of SEQ ID NO. 51, 52 and 53 and a VL containing CDRs of SEQ ID NOL. 54, 55 and 56.
Clone 212--FAP binding domain and variants thereof comprising the sequences as per claim 1.
Bacac et al discloses bispecific molecules comprising binding domain to FAP and OX40 and the use of these bispecific molecules for the treatment of cancer and that they can be used in combination with other bispecific molecules comprising binding domains to CD3 (summary, pages 9-13, 53-58 and entire reference). Bacac et al further teaches such bispecific molecules induce immune stimulation and stimulate tumor-specific T cell responses when administered to a subject (lines 5-30 on page 2, in particular). Bacac et al further teaches administering such bispecific molecules in combination with T-cell activating anti-CD3 bispecific antibodies to a subject with cancer in order to therapeutically treat the subject with both reagents (lines 11-19 on page 3, in particular). The clones for anti-FAP used is 28H1 and the clones used for anti-OX40 are 49B4, CLC-563 and 8H9 (which are the same clones as used in applicant’s claims and have the same sequences (pages 47-53 and 85-99 of WO document). Figure 1 discloses a 4+1 bispecific molecule comprising a tetravalent binding to OX40 and a monovalent binding to FAP. The bispecific molecules have an Fc region composed of a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 8 and 61-64). The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 67-74). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with anti-CD3 bispecific molecules (pages 75-84).
The only difference between the reference and the instant invention is the anti-FAP antibody being from clone 212 and variants thereof, the OX40 sequence from clone MOXR0916 and the bispecific structures as per claims 13-17.
Bruenker et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 84-90 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 44-60, 66-67 and 90-97 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 9-10). Pages 10-13 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 68-73). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 74-83).
Duerr et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 7-8, 73-78 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 40-50 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 50-55). Pages 5-6 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 58-63). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 64-72).
Du et al discloses anti-OX40 antibodies and their use in the treatment of cancer. The antibodies comprise CDRs of SEQ ID NO. 2-7 which are applicant’s SEQ ID NO. 43-48 respectively and VH of SEQ ID NO. 56 and VL of SEQ ID NO. 57 which are applicant VH and VL of SEQ ID NO. 49 and 50, respectively (summary, para. 432+ and entire reference). The antibodies can be used in the formation of bispecific antibodies (para 266). The reference also discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (para 294-300). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (para 338-429). The reference also discloses that the anti9-OX40 antibodies can be used in combination treatments for cancers wherein the combination is with anti-CD3 bispecific molecules, such as blinatumomab (para 423).
Since Bacac et al, Bruenker et al and Duerr et al are directed to using bispecific molecules for the treatment of cancer and since the references use an FAP binding domain in the bispecific and since FAP clone 212 and its variants are known in the art (Bruenker et al or Duerr et al), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to perform the method of Bacac et al of treating a subject with cancer by administering OX40/FAP bispecific antibodies to the subject in combination with T-cell activing anti-CD3 bispecific antibody of Bacac et al wherein the FAP binding domain of Bruenker et al or Duerr et al is used as the FAP binding domain of the OX40/FAP bispecific antibody of Bacac et al with the expected benefit of treating cancer. With respect to the use of OX40 clone MOXR0916 in the bispecific molecule, since the sequences of clone MOXR0916 are known and are used in the formation of bispecifics and used in the treatment of cancers (Du et al), it also would have been obvious to one of ordinary skill in the art to use the anti-OX40 clone of Du et al as the OX40 binding domain in Bacac et al, with the expected benefit of treating cancer. With respect to the specific bispecific structures of claims 13-17, both Bruenker et al and Duerr et al discloses the formation of these types of bispecific molecules. Thus, after modifying Bacac et al with the FAP clone 212 and its variants, it also would have been obvious to form said bispecific structures in view of Bruenker et al or Duerr et al.
Claim Rejections - 35 USC § 103
Claim(s) 1-28 is/are rejected under 35 U.S.C. 103 as being unpatentable over Amann et al WO 2017/055398 or US 10526413 (priority to 10/2/2015) in view of [{Bruenker et al WO 2020/070041 (priority to 10/1/2018) or US 11242396 (priority to 10/1/2018) or US 20200190207 (priority to 10/1/2018)} or {Duerr et al WO 2020/070035 (priority to 10/1/2018) or US 20210292426 (priority to 10/1/2018)}] and Du et al WO 2015/153513.
Amann et al discloses bispecific antibodies that bind OX40 and FAP for the treatment of cancer (summary, pages 57-62 and entire reference). Amann et al further teaches methods of treating a subject with cancer comprising administering such bispecific OX40/FAP antibodies in combination with a chemotherapeutic agent, radiation and/or other agents for use in cancer immunotherapy (paragraph spanning pages 13-14). Amann et al further teaches such antibodies stimulate tumor-specific T cell response when administered to a subject with cancer (lines 28-32 on page 94, in particular). The OX40 clones used are clones 8H9, 49B4 and CLC-563 and these are the same sequences as claimed in the instant applications (see pages 99+ of the WO document). Pages 66-71 disclose a 2+1 bispecific molecule comprising a bivalent binding to OX40 and a monovalent binding to FAP. The bispecific molecules have an Fc region composed of a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 71-75). The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 85-97). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other agents (pages 94-99).
The difference between the reference and the instant invention is the anti-FAP antibody being from clone 212 and variants thereof, the OX40 sequence from clone MOXR0916, the combination with anti-CD3 bispecific antibodies and the bispecific structures as per claims 13-17.
Bruenker et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 84-90 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 44-60, 66-67 and 90-97 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 9-10). Pages 10-13 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 68-73). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 74-83).
Duerr et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 7-8, 73-78 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 40-50 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 50-55). Pages 5-6 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 58-63). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 64-72).
Du et al discloses anti-OX40 antibodies and their use in the treatment of cancer. The antibodies comprise CDRs of SEQ ID NO. 2-7 which are applicant’s SEQ ID NO. 43-48 respectively and VH of SEQ ID NO. 56 and VL of SEQ ID NO. 57 which are applicant VH and VL of SEQ ID NO. 49 and 50, respectively (summary, para. 432+ and entire reference). The antibodies can be used in the formation of bispecific antibodies (para 266). The reference also discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (para 294-300). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (para 338-429). The reference also discloses that the anti-OX40 antibodies can be used in combination treatments for cancers wherein the combination is with anti-CD3 bispecific molecules, such as blinatumomab (para 423).
Since Amann et al, Bruenker et al and Duerr et al are directed to using bispecific molecules for the treatment of cancer and since both reference use an FAP binding domain in the bispecific and since FAP clone 212 and its variants are known in the art (Bruenker et al or Duerr et al), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the FAP binding domain of Bruenker et al or Duerr et al as the FAP binding domain in methods of treating subjects with cancer by administering OX40/FAP bispecific antibodies in combination with chemotherapy, radiation, and/or other cancer immunotherapeutics of Amann et al with the expected benefit of treating cancer. With respect to the use of OX40 clone MOXR0916 in the bispecific molecule, since the sequences of clone MOXR0916 are known and are used in the formation of bispecifics and used in the treatment of cancers (Du et al), it also would have been obvious to one of ordinary skill in the art to use the anti-OX40 clone of Du et al as the OX40 binding domain in Amann et al, with the expected benefit of treating cancer. With respect to the specific bispecific structures of claims 13-17, both Bruenker et al and Duerr et al discloses the formation of these types of bispecific molecules. Thus, after modifying Amann et al with the FAP clone 212 and its variants, it also would have been obvious to form said bispecific structures in view of Bruenker et al or Duerr et al. The addition of additional agents, such as anti-CD3 bispecific molecules, such as blinatumomab, is also obvious because Amann et al discloses that the bispecific molecules can be combined with other agents and because Du et al discloses that cancer therapy using anti-OX40 antibodies/bispecific antibodies can be combined with anti-CD3 antibodies.
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.
Claims 1-8 and 11-28 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of Amann et al U.S. Patent No. 10,526,413 in view of [{Bruenker et al WO 2020/070041 (priority to 10/1/2018) or US 11242396 (priority to 10/1/2018) or US 20200190207 (priority to 10/1/2018)} or {Duerr et al WO 2020/070035 (priority to 10/1/2018) or US 20210292426 (priority to 10/1/2018)}] and Du et al WO 2015/153513.
Amann et al claims antibodies to OX40 which comprise a VH comprising CDRs of SEQ ID No. 2, 4 and 7 and a VL comprising CDRs of SEQ ID NO. 13, 16 and 20. These are the same sequences that are in applicant’s clone 8H9. In view of (MPEP 804(II)(B)(2)(a), fifth paragraph) the Examiner is permitted to look at the specification for the definition of “antibodies” and as per col. 23, lines 49-54 these include bispecific antibodies. Thus, the claims are directed to bispecific antibodies comprising a VH comprising CDRs of SEQ ID No. 2, 4 and 7 and a VL comprising CDRs of SEQ ID NO. 13, 16 and 20. The claims also claim that the Fc region is of the IgG1 subclass and have L234A, L235A and P329G substitutions. The claims also state that the antibodies are used in pharmaceutical compositions. In view of Sun Pharmaceutical Industries v. Eli Lilly and Co., 611 F.3d 1381, 1389 (2010), the Examiner is allowed to look at the specification of the patent to determine the use of the claimed compound. The method in the patent discloses the use of the claimed patent compound in combination with other anti-cancer for the treatment of cancer, such chemotherapy or immunotherapy (lines 10-19 of column 11 and col. 77-81), which is the same in the instant application.
The only different between the claims and the instant set of claims is the FAP binding domain (clone 212 and its variants), the Fc bind IgG4, the polynucleotides and methods of making the bispecific molecule, the combination with anti-CD3 bispecific antibodies and the bispecific structures as per claims 13-17.
Bruenker et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 84-90 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 44-60, 66-67 and 90-97 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 9-10). Pages 10-13 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 68-73). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 74-83).
Duerr et al discloses bispecific molecules comprising binding domains to FAP and CD40 wherein the FAP binding domain is from clone 212 and variants thereof (these have the same sequences as those of applicant’s clone 212, see pages 7-8, 73-78 of WO document). The bispecific molecule comprises at least one binding domain of CD40 and at least one to OX40 and Figure 1 exemplified a 2+1 combination, 2 CD40 and one FAP) (also see summary, pages 40-50 and entire reference). The bispecific molecule comprises a Fc comprising a first and second subunit capable of stable association and wherein the Fc domain is IgG1Fc or IgG4 Fc and wherein the Fc domain can have L234A, L235A and P329G substitutions (pages 50-55). Pages 5-6 discloses applicant’s bispecific structures of claims 13-17. The reference discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (pages 58-63). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (pages 64-72).
Du et al discloses anti-OX40 antibodies and their use in the treatment of cancer. The antibodies comprise CDRs of SEQ ID NO. 2-7 which are applicant’s SEQ ID NO. 43-48 respectively and VH of SEQ ID NO. 56 and VL of SEQ ID NO. 57 which are applicant VH and VL of SEQ ID NO. 49 and 50, respectively (summary, para. 432+ and entire reference). The antibodies can be used in the formation of bispecific antibodies (para 266). The reference also discloses polynucleotides encoding said bispecific molecules and recombinant methods of making said antibodies (para 294-300). The reference discloses compositions comprising said bispecific antibodies and methods of using them to treat cancer and the treatment can be in combination with other therapeutic agents (para 338-429). The reference also discloses that the anti-OX40 antibodies can be used in combination treatments for cancers wherein the combination is with anti-CD3 bispecific molecules, such as blinatumomab (para 423).
Since the claims of Amann et al encompass bispecific antibodies and are used for the treatment of cancer and since Bruenker et al and Duerr et al are directed to using bispecific molecules for the treatment of cancer and since both reference use an FAP binding domain in the bispecific and since FAP clone 212 and its variants are known in the art (Bruenker et al or Duerr et al), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the FAP binding domain of Bruenker et al or Duerr et al as the FAP binding domain in Amann et al when administering OX40/FAP bispecific constructs in combination with other cancer therapies of Amann et al to subjects with cancer with the expected benefit of treating cancer. With respect to the specific bispecific structures of claims 13-17, both Bruenker et al and Duerr et al discloses the formation of these types of bispecific molecules. Thus, after modifying Amann et al with the FAP clone 212 and its variants, it also would have been obvious to form said bispecific structures in view of Bruenker et al or Duerr et al. Since Bruenker et al and Duerr et al discloses the polynucleotides and recombinant methods for making the bispecific antibodies, the making of the bispecific is obvious. Furthermore since Bruenker et al and Duerr et al discloses that Fc IgG1 and IgG4 can be used as the Fc region for the bispecific, the use of either Fc IgG is obvious. The addition of additional agents, such as anti-CD3 bispecific molecules, such as blinatumomab, is also obvious because Amann et al discloses that the bispecific molecules can be combined with other agents and because Du et al discloses that cancer therapy using anti-OX40 antibodies/bispecific antibodies can be combined with anti-CD3 antibodies.
Double Patenting
Claims 1-8 and 10-28 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. 11780919 B2. Although the claims at issue are not identical, they are not patentably distinct from each other because the patent claims are drawn to (i) compositions comprising bispecific antibodies encompassed by the instant claims; (ii) such compositions comprising said bispecific antibodies in combination with a chemotherapeutic, radiation, and/or other agent for use in cancer immunotherapy; and (iii) methods of treating a subject with cancer by administering said bispecific antibodies that are encompassed by methods of the instant claims. Further, one would have been motivated to treat a subject with cancer comprising administering to said subject a chemotherapeutic, radiation, and/or other agent for use in cancer immunotherapy when performing the method of treating the subject with cancer by performing the patented method of administering bispecific antibodies to the subject because one of skill in the art would recognize patients with cancer benefit from chemotherapeutics, radiation, and/or other agent for use in cancer immunotherapy.
Conclusion
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/SEAN E AEDER/Primary Examiner, Art Unit 1642