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 .
Status of the Claims
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are currently pending and are the subject of this Office Action. This is the first Office Action on the merits of the claims.
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 6 and 32 – 33 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 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 6 recites that the “VL and VH or the constant domains CL and CH of the Fab light chain and the Fab heavy chain are replaced by each other”. However, it is not clear which domain(s) is replaced and with what it/they are replaced with.
Claim 32, part (b), recites “(b) the first antigen binding domain is a Fab molecule wherein the variable domains VL and VH of the Fab light chain and the Fab heavy chain are replaced by each other”. However, it is not clear what domain(s) is/are replaced and with what and how the domains were arranged before the replacement(s).
Claim 33 depends from claim 32 and thus inherits the deficiencies of claim 32.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are rejected under 35 U.S.C. 103 as being unpatentable over WU (WO 2021/154534 A1, published 08/05/2021; see PTO-892: Notice of References Cited) in view of BRUENKER (WO 2021/255137 A1, filed 06/17/2021; see PTO-892).
The present application is directed to antibody that binds to CD3 and PLAP, wherein the antibody comprises (a) a first antigen binding domain that binds to CD3, comprising a heavy chain variable region (VH) comprising a heavy chain complementary determining region (HCDR) 1 comprising the amino acid sequence of SEQ ID NO: 2, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 3, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 6, and a light chain variable region (VL) comprising a light chain complementarity determining region (LCDR) 1 comprising the amino acid sequence of SEQ ID NO: 10, an LCDR 2 comprising the amino acid sequence of SEQ ID NO: 111 and an LCDR 3 comprising the amino acid sequence of SEQ ID NO: 12; and (b) a second antigen binding domain that binds to PLAP, comprising a VH comprising (i) an HCDR 1 comprising the amino acid sequence of SEQ ID NO: 28, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 29, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 30, (ii) an HCDR 1 comprising the amino acid sequence of SEQ ID NO: 32, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 33, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 34, (iii) an HCDR 1 comprising the amino acid sequence of SEQ ID NO: 36, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 37, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 38, (iv) an HCDR 1 comprising the amino acid sequence of SEQ ID NO: 40, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 41, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 42, or (v) an HCDR 1 comprising the amino acid sequence of SEQ ID NO: 44, an HCDR 2 comprising the amino acid sequence of SEQ ID NO: 45, and an HCDR 3 comprising the amino acid sequence of SEQ ID NO: 46, and a VL comprising an LCDR 1 comprising the amino acid sequence of SEQ ID NO: 48, an LCDR 2 comprising the amino acid sequence of SEQ ID NO: 49 and an LCDR 3 comprising the amino acid sequence of SEQ ID NO:50.
WU is directed to bispecific humanized PLAP (placental alkaline phosphatase)-CD3 epsilon chain (CD3e) antibodies, and a method for treating PLAP-positive cancer cells by administering the bispecific PLAP-CD3e antibody to the patients. See abstract. WU teaches that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells. See p. 1, lines 21 – 22.
WU discloses the PLAP-binding HCDRs of SEQ ID NOs: 28 – 30 and LCDRs of SEQ ID NOs: 48 – 50 of present claims 1, 16, and 32 with 100% identity. WU also discloses the anti-PLAP VH of SEQ ID NOs: 35 and anti-PLAP VL of SEQ ID NO: 51 of present claims 2, 3, 17, and 33 each with 100% identity. See Appendix.
BRUENKER is directed to a protease-activatable T cell activating bispecific molecule comprising a first antigen binding moiety capable of binding to CD3 for the treatment of cancer. See claims 1 and 47. BRUENKER discloses the CD3-binding HCDRs of SEQ ID NOs: 2, 3, and 6 and LCDRs of SEQ ID NOs: 10 – 12 with 100% identity. BRUENKER also discloses the anti-CD3 VH of SEQ ID NO: 9 and VL of SEQ ID NO: 13 of present claims 2, 3, and 33 each with 100% identity. See Appendix.
Because WU teaches a bispecific antibody targeting CD3 and PLAP (with the same anti-PLAP CDRs, VH, and VL of the present claims) for the treatment of cancer, and because BRUENKER discloses an antibody targeting CD3 (with the same anti-CD3 CDRs, VH, and VL of the present claims) for the treatment of cancer, it would have been obvious to one having ordinary skill in the art to modify WU’s bispecific antibody with BRUENKER’s anti-CD3 CDRs to arrive to the inventions of claims 1 – 3, 16 – 17, and 32 – 33. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
Regarding claims 4, 9, and 32, each appears to recite a structure of FIG. 1 of the drawings of the present specifications. For example, FIG. 1B, C, E, or F. However, WU teaches a similar structure. See WU’s FIG 1A (and p. 5, last paragraph) below:
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WU teaches a structure with a first and a second antigen-binding moiety each of which is a humanized Fab molecule, a human IgG Fc domain comprising a first subunit and a second subunit capable of stable association, with the CD3 binding domain (first antigen binding domain) and PLAP binding domain (second binding domain) are fused together, with the antibody further comprising a third antigen binding domain that binds to PLAP. See FIG 1A and p. 5, last paragraph.
In addition to the figure description, WU also describes a structure with a linker between the PLAP-binding domain and CD3-binding domain. See Construct #3, p. 15.
Regarding claims 6 and 32, WU teaches the use of CROSSFAB approach, which crossovers the constant domain and variable domain and switches the CHI domain and CL domain in the CD3e Fab molecule, which reduces undesired mis-paring. See p. 6, lines 19 – 21. WU also teaches a second antigen binding domain that is a conventional Fab molecule. See FIG 1A and p. 5, last paragraph.
Regarding claim 8 and 32, BRUENKER teaches that to improve correct pairing of the light chains with the corresponding heavy chains, mutations were introduced in the human CL (E123R, Q124K) and the human CHI (K147E, K213E) of the TYRP1 binding Fab molecule. See p. 119, lines 3 – 5.
Regarding claims 9 and 32, according to the specification, WU teaches a structure LAP h4 VH-CH1- Fc (knob) P329GLA-LA-CD3VH-linker-VL Amino acids of PLAP h4 VH-CH1, see Example 3, part of Construct 3.
Regarding claims 10 and 11, WU discloses a structure with (from N-to-C terminus) with PLAP Fab connected to CD3 Fab. See p. 15, Construct #3.
Regarding claims 12 and 32, WU discloses mutations of S354C and T366W on one Fc, and the corresponding “hole” is made by mutations of Y349C, T366S, L368A and Y407V on the partner Fc. See p. 7, lines 28 – 30.
Regarding claims 18 – 21, WU teaches that the nucleic acid encoding the disclosed bispecific antibody can be inserted into a vector and expressed in mammalian 293 S or CHO cells using serum-free medium and can be purified with protein A or protein G column and used for the study. See p. 9, lines 7 – 10 and p. 10, lines 10 – 32.
Regarding claim 29, WU teaches a pharmaceutical composition comprising the bispecific antigen-binding molecule and a pharmaceutically acceptable carrier. See p. 9, lines 5 – 6.
Regarding claim 34, BRUENKER teaches a method of treating or delaying progression of an immune related disease, or enhancing or stimulating an immune response or function in an individual (see p. 10, lines 4 – 6) and thus renders the treatment of an autoimmune disease obvious.
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 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 – 91 of U.S. Patent No. 12,466,889 in view of WU and BRUENKER.
Patented claim 1 recites a bispecific antibody that binds to human HLA-G and human CD3.
Patented claim 22 recites that the bispecific comprises a polypeptide comprising an amino acid sequence that is at least 98% identical to the sequence of SEQ ID NO: 79.
Patented claim 40 recites a polypeptide comprising an amino acid sequence that is at least 98% identical to the sequence of SEQ ID NO: 76, wherein the polypeptide comprises, in an N- to C-terminal direction, the VH domain comprising the amino acid sequence of SEQ ID NO: 58.
Patented SEQ ID NOs: 79 discloses the CDRs of present SEQ ID NOs: 10 – 12 with 100% identity. Patented SEQ ID NOs: 76 and 58 each discloses the CDRs of present SEQ ID NOs: 2, 3, and 6 with 100% identity. See Appendix.
The main difference between the present claims and the patented claims is that the present claims recite that the bispecific antibody binds PLAP instead of HLA-G. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the patented claims recite a bispecific antibody that binds to human HLA-G and human CD3 (including the CD3-binding CDRs of the present claims) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the patented claims’ CD3 domain in WU’s bispecific antibody that binds to PLAP and CD3, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells and tumor associated antigen is a common approach to bringing cytotoxic T cells to kill cancer cells, as evidenced by the prior art.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3, 6, 61 – 114, 116 – 128, and 130 – 131 of copending Application No. 17/448,729 in view of WU and BRUENKER.
Copending claim 3 recites a method for treatment of a cancer or an autoimmune disease in an individual, wherein said method comprises;(a) the administration of a T cell bispecific antibody to the individual, wherein the T cell bispecific antibody comprises an Fc domain composed of a first and a second subunit, and (b) the administration of a tyrosine kinase inhibitor (TKI) to the individual for the prevention or mitigation of an adverse effect related to the administration of the T cell bispecific antibodyl wherein the TKI is first administered prior to administration of the T cell bispecific antibody.
Copending claim 85 recites that the T cell bispecific antibody comprises an antigen binding moiety that binds to CD3 and an antigen binding moiety that binds to a target cell antigen.
Copending claim 90 recites a light chain variable region sequence that is at least about 95% identical to the amino acid sequence of SEQ ID NO: 35.
Copending claim 111 recites heavy chain variable region sequence that is at least about 95% identical to the amino acid sequence of SEQ ID NO: 66.
Copending SEQ ID NO: 35 discloses the CDRs of present SEQ ID NO: 10 – 12, and copending SEQ ID NO: 66 discloses the CDRs of present SEQ ID NOs: 2, 3, and 6 with 100% identity. See Appendix.
The main difference between the present claims and the copending claims is that the present claims recite that the bispecific antibody binds PLAP. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the copending claims recite a bispecific antibody that binds CD3 (including the CD3-binding CDRs) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the copending claims’ CD3 domain in WU’s anti-PLAP x anti-CD3 bispecific antibody, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
This is a provisional nonstatutory double patenting rejection.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 59 – 60, 63 – 71, and 74 – 103 of copending Application No. 17/454,193 in view of WU and BRUENKER.
Copending claim 59 recites a method for preventing or mitigating an adverse effect related to the administration of a T cell bispecific antibody to an individual, comprising administering (a) a T cell bispecific antibody and (b) an inhibitor that inhibits mTOR signaling to the individual, wherein the adverse effect is prevented or mitigated, wherein the T cell bispecific antibody binds to CD3 and a target cell antigen, and wherein the method does not comprise administering a CAR-T cell, and wherein administering the inhibitor that inhibits mTOR signaling causes inhibition of an adverse effect related to administering the T cell bispecific antibody.
Copending claim 78 recites that the light chain variable region sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to an amino acid sequence of SEQ ID NO: 11.
Copending claim 95 recites that the first antigen binding moiety comprises a heavy chain variable region sequence that is at least about 95%, 96%, 97%, 98%, 99% or 100% identical to an amino acid sequence of SEQ ID NO: 63or SEQ ID NO: 66.
Copending SEQ ID NO: 11 discloses the CDRs of present SEQ ID NOs: 10 – 12, and copending SEQ ID NO: 66 discloses the CDRs of present SEQ ID NOs: 2, 3, and 6 with 100% identity. See Appendix.
The main difference between the present claims and the copending claims is that the present claims recite that the bispecific antibody binds PLAP. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the copending claims recite a bispecific antibody that binds CD3 (including the CD3-binding CDRs) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the copending claims’ CD3 domain in WU’s anti-PLAP x anti-CD3 bispecific antibody, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
This is a provisional nonstatutory double patenting rejection.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 – 51 of copending Application No. 18/066,529 in view of WU and BRUENKER.
Copending claim 1 recites a protease-activatable T cell activating bispecific molecule comprising (a) a first antigen binding moiety capable of binding to CD3.
Copending claim 2 recites that the protease-activatable T cell activating bispecific molecule of claim 1, wherein the VH comprises an amino acid sequence that is at least about 95%, 96%, 97%,98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 16, , and/or the VL comprises an amino acid sequence that is at least about 95% 96%, 97%,98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO: 23.
Copending SEQ ID NO: 16 discloses the CDRs of present SEQ ID NOs: SEQ ID NOs: 2, 3, and 6, and copending SEQ ID NO: 23 discloses the CDRs of present 10 – 12 with 100% identity. See Appendix.
The main difference between the present claims and the copending claims is that the present claims recite that the bispecific antibody binds PLAP. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the copending claims recite a bispecific antibody that binds CD3 (including the CD3-binding CDRs) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the copending claims’ CD3 domain in WU’s anti-PLAP x anti-CD3 bispecific antibody, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
This is a provisional nonstatutory double patenting rejection.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 9 – 10, 12 – 15, 17, 21 – 22, 24 – 25, 27 – 28, 32 – 33, 38 , 41, 46 – 48, 53 – 55, 57, 62 – 63, 68, 70 – 74, 76, 84 – 86, and 90 of copending Application No. 18/067,330 in view of WU and BRUENKER.
Copending claim 1 recites an immune activating fragment crystallizable (Fc) domain binding molecule comprising (a) an Fc domain binding moiety that specifically binds to a target Fc domain comprising a first set of at least one amino acid substitution that reduces binding affinity to an Fc receptor and/or effector function, wherein the first set of at least one amino acid substitution comprises the amino acid substitution P329G (numberings according to Kabat EU index) (b) an immune activating moiety, and(c) a half-life extending Fc domain, wherein the half-life extending Fc domain comprises a second set of at least one amino acid substitution that reduces binding affinity to an Fc receptor and/or effector function, wherein the second set of at least one amino acid substitution comprises a substitution at position P329 by an amino acid other than glycine (G) (numbering according to Kabat EU index), and wherein the Fc domain binding moiety does not specifically bind to the half-life extending Fc domain.
Copending claim 38 a second heavy chain comprising the amino acid sequence having at least identity to SEQ ID NO:179.
Copending claim 53 recites a heavy chain variable region comprising an amino acid sequence having at least identity to the amino acid sequence of SEQ ID NO: 49.
Copending SEQ ID NO: 179 discloses the CDRs of present 10 – 12, and copending SEQ ID NO: 49 discloses the CDRs of present SEQ ID NOs: SEQ ID NOs: 2, 3, and 6, and copending with 100% identity. See Appendix.
The main difference between the present claims and the copending claims is that the present claims recite that the bispecific antibody binds PLAP. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the copending claims recite a bispecific antibody that binds CD3 (including the CD3-binding CDRs) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the copending claims’ CD3 domain in WU’s anti-PLAP x anti-CD3 bispecific antibody, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
This is a provisional nonstatutory double patenting rejection.
Claims 1 – 4, 6, 8 – 12, 16 – 22, 29, and 32 – 34 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 5 – 12, 18, 21 – 25, 30 – 33, and 42 of copending Application No. 18/069,847 in view of WU and BRUENKER.
Copending claim 1 recites a bispecific agonistic CD28 antigen binding molecule characterized by monovalent binding to CD28, comprising (a) a first antigen binding domain capable of specific binding to CD28, (b) a second antigen binding domain capable of specific binding to CD3.
Copending claim 9 recites that the bispecific agonistic CD28 antigen binding molecule of claim 1, wherein the antigen binding domain capable of specific binding to CD3 comprises the CDRs of the heavy chain variable region (VHCD3) comprising the amino acid sequence of SEQ ID NO:16 and the CDRs of the light chain variable region (VLCD3) comprising the amino acid sequence of SEQ ID NO:17.
Copending claim 10 recites that the bispecific agonistic CD28 antigen binding molecule of claim 1,wherein the antigen binding domain capable of specific binding to CD3 comprises a heavy chain variable region (VHCD3) comprising the amino acid sequence of SEQ ID NO:16, and a light chain variable region (VLCD3) comprising the amino acid sequence of SEQ ID NO:17.
The main difference between the present claims and the copending claims is that the present claims recite that the bispecific antibody binds PLAP. However, WU discloses this difference. The teachings of WU and BRUENKER, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 103 above.
Because the copending claims recite a bispecific antibody that binds CD3 (including the CD3-binding CDRs) for the treatment of cancer and WU teaches a bispecific antibody that binds to human PLAP and human CD3, it would have been obvious to one having ordinary skill in the art to use the copending claims’ CD3 domain in WU’s anti-PLAP x anti-CD3 bispecific antibody, thereby arriving to the bispecific antibody of the present claims. There would have been a reasonable expectation of success considering that using bispecific antibodies binding T cells (such as via CD3) and tumor associated antigen (such as PLAP) is the most common approach to design bispecific antibody by bringing cytotoxic T cells to kill cancer cells, as evidenced by applied prior art.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ESTELLA M. GUSTILO whose telephone number is (703)756-1706. The examiner can normally be reached Monday - Friday 9:00 AM - 5:00 PM.
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/ESTELLA M. GUSTILO/Examiner, Art Unit 1646
/PETER J REDDIG/Primary Examiner, Art Unit 1646
APPENDIX
Alignment with SEQ ID NOs: 2, 3, and 6
RESULT 1
BKL74815
(NOTE: this sequence has 18 duplicates in the database searched.
See complete list at the end of this report)
ID BKL74815 standard; protein; 125 AA.
XX
AC BKL74815;
XX
DT 16-JUN-2022 (revised)
DT 10-FEB-2022 (first entry)
XX
DE Anti-CD3 antibody CD3opt (P035.093) VH region, SEQ ID 16.
XX
KW CD3; antibody; antibody production; antibody therapy; cancer; cytostatic;
KW heavy chain variable region; immune disorder; immunomodulator;
KW therapeutic.
XX
OS Unidentified.
OS Synthetic.
XX
CC PN WO2021255137-A1.
XX
CC PD 23-DEC-2021.
XX
CC PF 17-JUN-2021; 2021WO-EP066335.
XX
PR 19-JUN-2020; 2020EP-00181072.
XX
CC PA (HOFF ) HOFFMANN LA ROCHE & CO AG F.
CC PA (HOFF ) HOFFMANN LA ROCHE INC.
XX
CC PI Bruenker P, Carpy Gutierrez Cirlos A, Freimoser-Grundschober A;
CC PI Geiger M, Hofer T, Klein C, Moessner E, Neumann C;
XX
DR WPI; 2021-E8034L/007.
XX
CC PT Protease-activatable T cell activating bispecific molecule for treating
CC PT disease such as cancer, comprises first and second antigen binding
CC PT moiety, masking moiety covalently attached to T cell bispecific binding
CC PT molecule.
XX
CC PS Claim 2; SEQ ID NO 16; 181pp; English.
XX
CC The present invention relates to a novel protease-activatable T cell
CC activating bispecific molecule useful for treating disease such as
CC cancer. The protease-activatable T cell activating bispecific molecule
CC comprises a first antigen binding moiety capable of binding to CD3, a
CC second antigen binding moiety capable of binding to a target cell
CC antigen, and a masking moiety. The invention further provides: an
CC idiotype-specific polypeptide capable of reversibly concealing an anti-
CC CD3 antigen binding site of a molecule; a pharmaceutical composition
CC comprising the protease-activatable T cell activating bispecific molecule
CC or the idiotype-specific polypeptide and a pharmaceutically acceptable
CC carrier; an isolated polynucleotide encoding the protease-activatable T
CC cell activating bispecific antigen binding molecule or idiotype-specific
CC polypeptide; a vector comprising the polynucleotide; a host cell
CC comprising the polynucleotide or the vector; a method for producing the
CC protease-activatable T cell activating bispecific molecule; the use of
CC the protease-activatable T cell activating bispecific molecule or the
CC idiotype-specific polypeptide for manufacturing a medicament for treating
CC diseases such as cancer, immune related disease or immune response or
CC function related disease; and a method for treating diseases in an
CC individual by administering a therapeutically effective amount of the
CC pharmaceutical composition comprising the protease-activatable T cell
CC activating bispecific molecule.
CC
CC Revised record issued on 16-JUN-2022 : Addition of DWPI-enhanced title
CC (PT field).
XX
SQ Sequence 125 AA;
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-047-605-58
Filing date in PALM: 2022-10-18
Sequence 58, US/18047605
Publication No. US20230159642A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Anti-HLA-G antibodies and use thereof (en)
FILE REFERENCE: 50474-285002
CURRENT APPLICATION NUMBER: US/18/047,605
CURRENT FILING DATE: 2022-10-18
NUMBER OF SEQ ID NOS: 96
SEQ ID NO 58
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
note = heavy chain variable domain VH, P035-093
organism = synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-17-448-729-66
Filing date in PALM: 2021-09-24
Sequence 66, US/17448729
Publication No. US20220088195A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc.
TITLE OF INVENTION: Prevention or mitigation of T-cell bispecific antibody-related
TITLE OF INVENTION: adverse effects
FILE REFERENCE: P36412-US
CURRENT APPLICATION NUMBER: US/17/448,729
CURRENT FILING DATE: 2021-09-24
PRIOR APPLICATION NUMBER: EP20198050.5
PRIOR FILING DATE: 2020-09-24
PRIOR APPLICATION NUMBER: EP20201583.0
PRIOR FILING DATE: 2020-10-13
PRIOR APPLICATION NUMBER: EP21172627.8
PRIOR FILING DATE: 2021-05-07
NUMBER OF SEQ ID NOS: 81
SEQ ID NO 66
LENGTH: 125
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-17-454-193-66
Filing date in PALM: 2021-11-09
Sequence 66, US/17454193
Publication No. US20220168418A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc.
TITLE OF INVENTION: Prevention or mitigation of T-cell engaging agent-related adverse
TITLE OF INVENTION: effects
FILE REFERENCE: P36507-US
CURRENT APPLICATION NUMBER: US/17/454,193
CURRENT FILING DATE: 2021-11-09
PRIOR APPLICATION NUMBER: EP20206567.8
PRIOR FILING DATE: 2020-11-10
PRIOR APPLICATION NUMBER: EP21155823.4
PRIOR FILING DATE: 2021-02-08
PRIOR APPLICATION NUMBER: EP21172623.7
PRIOR FILING DATE: 2021-05-07
PRIOR APPLICATION NUMBER: EP21187472.2
PRIOR FILING DATE: 2021-07-23
NUMBER OF SEQ ID NOS: 80
SEQ ID NO 66
LENGTH: 125
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-047-605-58
Filing date in PALM: 2022-10-18
Sequence 58, US/18047605
Publication No. US20230159642A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Anti-HLA-G antibodies and use thereof (en)
FILE REFERENCE: 50474-285002
CURRENT APPLICATION NUMBER: US/18/047,605
CURRENT FILING DATE: 2022-10-18
NUMBER OF SEQ ID NOS: 96
SEQ ID NO 58
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
note = heavy chain variable domain VH, P035-093
organism = synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-047-605-76
Filing date in PALM: 2022-10-18
Sequence 76, US/18047605
Publication No. US20230159642A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Anti-HLA-G antibodies and use thereof (en)
FILE REFERENCE: 50474-285002
CURRENT APPLICATION NUMBER: US/18/047,605
CURRENT FILING DATE: 2022-10-18
NUMBER OF SEQ ID NOS: 96
SEQ ID NO 76
LENGTH: 232
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..232
QUALIFIERS: mol_type = protein
note = light chain 1 P1AF7977
organism = synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 232;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-066-529-16
Filing date in PALM: 2022-12-15
Sequence 16, US/18066529
Publication No. US20230287145A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Protease-activated T cell bispecific antibodies (en)
FILE REFERENCE: P36114-US
CURRENT APPLICATION NUMBER: US/18/066,529
CURRENT FILING DATE: 2022-12-15
NUMBER OF SEQ ID NOS: 127
SEQ ID NO 16
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..125
QUALIFIERS: note = CD3opt VH (P035.093)
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-067-330-49
Filing date in PALM: 2022-12-16
Sequence 49, US/18067330
Publication No. US20240043535A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Immune activating Fc domain binding molecules (en)
FILE REFERENCE: P36106-US
CURRENT APPLICATION NUMBER: US/18/067,330
CURRENT FILING DATE: 2022-12-16
NUMBER OF SEQ ID NOS: 180
SEQ ID NO 49
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..125
QUALIFIERS: note = Synthetic construct
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-067-330-70
Filing date in PALM: 2022-12-16
Sequence 70, US/18067330
Publication No. US20240043535A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Immune activating Fc domain binding molecules (en)
FILE REFERENCE: P36106-US
CURRENT APPLICATION NUMBER: US/18/067,330
CURRENT FILING DATE: 2022-12-16
NUMBER OF SEQ ID NOS: 180
SEQ ID NO 70
LENGTH: 232
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..232
QUALIFIERS: note = Synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 232;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
US-18-069-847-16
Filing date in PALM: 2022-12-21
Sequence 16, US/18069847
Publication No. US20230416366A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Anti-CD3/anti-CD28 bispecific antigen binding molecules (en)
FILE REFERENCE: P36198-US
CURRENT APPLICATION NUMBER: US/18/069,847
CURRENT FILING DATE: 2022-12-21
NUMBER OF SEQ ID NOS: 212
SEQ ID NO 16
LENGTH: 125
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..125
QUALIFIERS: note = heavy chain variable domain VH, CD3 (P035.093)
FEATURE:
NAME/KEY: source
LOCATION: 1..125
QUALIFIERS: mol_type = protein
organism = synthetic construct
ALIGNMENT:
Query Match 87.8%; Score 176.4; Length 125;
Best Local Similarity 45.2%;
Matches 38; Conservative 0; Mismatches 0; Indels 46; Gaps 2;
Qy 1 SYAMN--------------RIRSKYNNYATYYADSVKG---------------------- 24
||||| |||||||||||||||||||
Db 31 SYAMNWVRQAPGKGLEWVSRIRSKYNNYATYYADSVKGRFTISRDDSKNTLYLQMNSLRA 90
Qy 25 ----------ASNFPASYVSYFAY 38
||||||||||||||
Db 91 EDTAVYYCVRASNFPASYVSYFAY 114
Alignment with SEQ ID NOs: 10 – 12
BKL74822
ID BKL74822 standard; protein; 109 AA.
XX
AC BKL74822;
XX
DT 16-JUN-2022 (revised)
DT 10-FEB-2022 (first entry)
XX
DE Anti-CD3 antibody CD3orig/CD3opt VL region, SEQ ID 23.
XX
KW CD3; antibody; antibody production; antibody therapy; cancer; cytostatic;
KW immune disorder; immunomodulator; light chain variable region;
KW therapeutic.
XX
OS Unidentified.
OS Synthetic.
XX
CC PN WO2021255137-A1.
XX
CC PD 23-DEC-2021.
XX
CC PF 17-JUN-2021; 2021WO-EP066335.
XX
PR 19-JUN-2020; 2020EP-00181072.
XX
CC PA (HOFF ) HOFFMANN LA ROCHE & CO AG F.
CC PA (HOFF ) HOFFMANN LA ROCHE INC.
XX
CC PI Bruenker P, Carpy Gutierrez Cirlos A, Freimoser-Grundschober A;
CC PI Geiger M, Hofer T, Klein C, Moessner E, Neumann C;
XX
DR WPI; 2021-E8034L/007.
XX
CC PT Protease-activatable T cell activating bispecific molecule for treating
CC PT disease such as cancer, comprises first and second antigen binding
CC PT moiety, masking moiety covalently attached to T cell bispecific binding
CC PT molecule.
XX
CC PS Claim 2; SEQ ID NO 23; 181pp; English.
XX
CC The present invention relates to a novel protease-activatable T cell
CC activating bispecific molecule useful for treating disease such as
CC cancer. The protease-activatable T cell activating bispecific molecule
CC comprises a first antigen binding moiety capable of binding to CD3, a
CC second antigen binding moiety capable of binding to a target cell
CC antigen, and a masking moiety. The invention further provides: an
CC idiotype-specific polypeptide capable of reversibly concealing an anti-
CC CD3 antigen binding site of a molecule; a pharmaceutical composition
CC comprising the protease-activatable T cell activating bispecific molecule
CC or the idiotype-specific polypeptide and a pharmaceutically acceptable
CC carrier; an isolated polynucleotide encoding the protease-activatable T
CC cell activating bispecific antigen binding molecule or idiotype-specific
CC polypeptide; a vector comprising the polynucleotide; a host cell
CC comprising the polynucleotide or the vector; a method for producing the
CC protease-activatable T cell activating bispecific molecule; the use of
CC the protease-activatable T cell activating bispecific molecule or the
CC idiotype-specific polypeptide for manufacturing a medicament for treating
CC diseases such as cancer, immune related disease or immune response or
CC function related disease; and a method for treating diseases in an
CC individual by administering a therapeutically effective amount of the
CC pharmaceutical composition comprising the protease-activatable T cell
CC activating bispecific molecule.
CC
CC Revised record issued on 16-JUN-2022 : Addition of DWPI-enhanced title
CC (PT field).
XX
SQ Sequence 109 AA;
ALIGNMENT:
Query Match 84.8%; Score 138.3; Length 109;
Best Local Similarity 39.0%;
Matches 30; Conservative 0; Mismatches 0; Indels 47; Gaps 2;
Qy 1 GSSTGAVTTSNYAN---------------GTNKRAP------------------------ 21
|||||||||||||| |||||||
Db 23 GSSTGAVTTSNYANWVQEKPGQAFRGLIGGTNKRAPGTPARFSGSLLGGKAALTLSGAQP 82
Qy 22 --------ALWYSNLWV 30
|||||||||
Db 83 EDEAEYYCALWYSNLWV 99
US-18-047-605-79
Filing date in PALM: 2022-10-18
Sequence 79, US/18047605
Publication No. US20230159642A1
GENERAL INFORMATION
APPLICANT: Hoffmann-La Roche Inc. (en)
TITLE OF INVENTION: Anti-HLA-G antibodies and use thereof (en)
FILE REFERENCE: 50474-285002
CURRENT APPLICATION NUMBER: US/18/047,605
CURRENT FILING DATE: 2022-10-18
NUMBER OF SEQ ID NOS: 96
SEQ ID NO 79
LENGTH: 674
TYPE: PRT
FEATURE:
NAME/KEY: source
LOCATION: 1..674
QUALIFIERS: mol_type = protein
note = heavy chain 2 P1AF7977
organism = synthetic construct
ALIGNMENT:
Query Match 84.8%; Score 138.3; Length 674;
Best Local Similarity 39.0%;
Matches 30; Conservative 0; Mismatches 0; Indels 47; Gaps 2;
Qy 1 GSSTGAVTTSNYAN---------------GTNKRAP------------------------