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 .
DETAILED ACTION
Applicant’s election without traverse of Group I, claims 1, 2, 4, 9, 10, 14, and 21, as well as the species election of 1) a cytotoxic T cell as a species of T cell type and 2) GD2 as a species of target antigen, in the reply filed on 03/25/2026 is acknowledged.
Claims 1, 2, 4, 9, 10, 14, 21, 26, 28, 30, 33, 36, 38, 45, 46, 48, 51, 56, 57, and 60 are pending.
Claims 26, 28, 30, 33, 36, 38, 45, 46, 48, 51, 56, 57, and 60 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 03/25/2026.
Claims 4 and 14 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 03/25/2026.
Claims 1, 2, 9, 10, and 21 are under examination on the merits.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Claims 1, 2, 9, 10, and 21 have an effective filing date of 07/28/2020, corresponding to PRO 63/057,871.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 01/27/2023 and 12/27/2024 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Rejections
35 U.S.C. 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 21 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116.
Claim 21 is drawn to an anti-CD3 antibody that comprises a heavy chain SEQ ID NO and/or a light chain SEQ ID NO, or variants of said heavy chain SEQ ID NO and light chain SEQ ID NO comprising one or more conservative amino acid substitutions.
The claim encompasses a genus of anti-CD3 antibodies having diverse heavy and light chain CDR amino acid sequences. Following a review of the specification, it appears that Applicant has disclosed numerous species within the claimed genus, specifically the heavy chain/light chain combinations recited in claim 21; however in view of this disclosure, Applicant is claiming a broad genus of molecules that would be expected to encompass multiple anti-CD3 binding domains having diverse heavy and light chain CDR sequences. Even though Applicant has disclosed numerous species within said genus, the specification does not provide adequate written description for the entire claimed genus, because one skilled in the art would be unable to immediately envision, recognize, or distinguish at least most of the members comprised within the genus claimed, specifically, which light and heavy chain CDR sequence variants (and combinations of said CDR sequence variants) give rise to antibody molecules capable of binding CD3. As detailed below Applicant’s disclosure is not sufficient to demonstrate possession of the entire claimed genus, and as such Applicant’s disclosure does not satisfy the written description requirement of 35 U.S.C. 112(a).
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
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A “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. In the instant case, Applicant has disclosed numerous species within the genus claimed; however given the substantial antibody structure variation within the genus, as well as the high level of unpredictability in the art, the disclosure of said species comprised within the claimed genus is not sufficiently representative of the entire genus.
Furthermore Applicant has not disclosed relevant, identifying characteristics of CDR region amino acid sequence variants (or combinations thereof) that confer upon an antibody the ability to bind CD3, because the instant specification does not provide structural antibody features that correlate with a functional ability to bind CD3. To elaborate on why the claimed antibodies lack adequate written description, Mariuzza (Annu. Rev. Biophys. Biophys. Chem., 16: 139-159, 1987) reviews the structural basis of antigen-antibody recognition and teach that naturally occurring conventional antibodies comprise two polypeptides, the so-called light and heavy chains. The antigen-combining site of an antibody is a three-dimensional structure that fully comprises six CDRs, three each from the light and heavy chains. The amino acid sequences of the CDRs are hypervariable, as the amino acid residues contained within the CDRs determine much of the antibody’s antigen-binding specificity. In view of Mariuzza, it is apparent that antibodies having less than all six CDRs that form the antigen binding site of a conventional antibody in their proper context of heavy and light chain variable domains do not describe the particularly identifying structural feature of the antibody that correlates with the antibody’s ability to bind antigen. Absent a description of the at least minimal structural features correlating with a functional ability to bind CD3 which are shared by members of a genus commonly sharing this function, it is submitted that the skilled artisan could not immediately envision, recognize, or distinguish which heavy and light chain CDR amino acid sequences (or combinations thereof) may be combined such that the resultant heavy and light chain variable regions comprise six CDRs that confer the ability to bind CD3.
Furthermore while the prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is noted that the art is characterized by a high level of unpredictability, since the skilled artisan still cannot accurately and reliably predict the consequences of amino acid substitutions, insertions, and deletions in the antigen-binding domains. For example in a series of experiments involving a monoclonal antibody to Legionella pneumophilia serotype 1, McCarthy et al. (J. Immunol. Methods, 251(1-2): 137-149, 2001) demonstrated that a single VH CDR3 substitution of tyrosine to serine at position 95 resulted in the total loss of antigen recognition in an ELISA. Lin et al. (African Journal of Biotechnology, 10(79):18294-18302, 2011) teach that a single amino acid substitution in the VL CDR3 of an anti-avian infectious bronchitis virus (IBV) single-chain antibody (ZL.80) may abrogate binding. For example at Figure 3, Lin et al. demonstrate that replacing either the Cys105 or Asp106 residue in the VL CDR3 of ZL.80 with an alanine residue reduces binding to near negative control levels. Lin et al. also teach that some single amino acid substitutions in the VL CDR3 of ZL.80 may significantly improve binding. For example replacing the Val108 residue in the VL CDR3 of ZL.80 with a tyrosine residue results in a 12.9-fold increase in affinity compared to parental ZL.80. Accordingly absent empirical determination, one skilled in the art would be unable to predict or envision which CDR residues of the recited heavy and light chain sequences could be changed such that the resultant variant CDR residues form an antigen-binding site capable of binding CD3. The general knowledge and level of skill in the art does not adequately supplement the omitted description, because specific, not general, guidance is needed. Since the disclosure fails to describe relevant, identifying structural characteristics, in the form of heavy and light chain CDR amino acid sequences, that correlate with the ability to bind CD3, and because the two disclosed species detailed above are not sufficient to describe the claimed genus, it is submitted that the written description requirement of 35 U.S.C. 112(a) has not been met.
Although screening techniques can be used to isolate CDR variant antibodies that possess the ability to bind CD3, Applicant is reminded that the written description requirement of 35 U.S.C. 112 is severable from the enablement provision. As stated in Vas-Cath Inc. v. Mahurkar (CA FC) 19 USPQ2d 1111, 935 F2d 1555, “The purpose of the ‘written description’ requirement is broader than to merely explain how to ‘make and use’; the applicant must also convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.”
It is also noted that claim 21 recites an anti-CD3 antibody having a heavy chain amino acid sequence and/or a light chain amino acid sequence. This is problematic with respect to 35 U.S.C. 112(a), because absent empirical determination, one skilled in the art would be unable to readily determine which light chain amino acid sequence may be combined with the recited heavy chain amino acid sequences such that a resultant antigen-binding region is capable of binding to CD3. Likewise absent empirical determination, one skilled in the art would be unable to readily determine which heavy chain amino acid sequence may be combined with the recited light chain amino acid sequences such that a resultant antigen-binding region is capable of binding to CD3.
Accordingly given the unpredictability associated with antibody CDR region changes on antigen binding and given the lack of particularity with which the claimed antibodies are described in the specification, it is submitted that the skilled artisan could not immediately envision, recognize, or distinguish at least most of the members of the genus to which the claims are directed, and therefore the specification would not reasonably convey to the skilled artisan that Applicant was in possession of the claimed invention at the time the application was filed.
35 U.S.C. 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, 2, 9, and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Park et al. (Blood, Adoptive Immunotherapy: Poster III, November 2018, in IDS from 01/27/2023) in view of Chang et al. (US PG PUB 2014/0050660, publication date: 02/20/2014), Cheung et al. (WO 2016/014942, international publication date: 01/28/2016), and Carter et al. (US 2010/0105136, publication date: 04/29/2010).
Park et al. teach that “T-cell based therapies have emerged as one of the major breakthroughs in anticancer treatment: Immune checkpoint inhibitors, chimeric antigen receptor gene-modified T-cells (CAR-T-cells), and T-cell engaging bispecific antibodies (BsAb) are leading the advances. In the era of personalized medicine, T-cells offer alternative strategies to overcome resistance to chemotherapy or small molecules. Yet, hurdles for such therapy can be crippling, such as inability of T cells to infiltrate “cold tumors”, cytokine release syndrome following T cell-based therapies, neurologic toxicity, and on-target off-tumor effects. To address these hurdles, polyclonal T-cells armed with GD2xCD3 or HER2xCD3 BsAb for cytotherapy hold promise. Ganglioside GD2 and HER2 are tumor associated surface antigens expressed in a broad spectrum of aggressive malignancies, while being restricted in normal tissues.” See Introduction. In the Methods section, Park et al. teach that “[r]ecombinant anti-GD2 BsAb and anti-HER2 BsAb were made using the IgG(L)-scFv platform (Can Immunol Res, 3:266, 2015, Oncoimmunology, PMID:28405494). T-cells from normal volunteer donors were isolated, activated and expanded by CD3/CD28 beads in the presence of 100 IU/mL of interleukin 2 (IL-2).” Given that the experiments of Park et al. involved T cells isolated from volunteers, said T cells would be expected to comprise CD8 T cells (cytotoxic T cells) and CD4 T cells (helper T cells), and said T cells appear to be armed ex vivo.
As such Park et al. teach an ex vivo armed T cell that is coated or complexed with an effective arming dose of at least one type of anti-CD3 multi-specific antibody, wherein the at least one type of anti-CD3 multi-specific antibody includes a CD3 binding domain comprising a heavy chain immunoglobulin variable domain (VH) and a light chain immunoglobulin variable domain (VL); however Park et al. do not teach or suggest an ex vivo armed T cell that is coated or complexed with an effective arming dose of at least one type of anti-CD3 multi-specific antibody, wherein the at least one type of anti-CD3 multi-specific antibody includes a CD3 binding domain comprising a heavy chain immunoglobulin variable domain (VH) and a light chain immunoglobulin variable domain (VL), wherein (a) the VH comprises a VH-CDR1 sequence of SEQ ID NO: 1, a VH-CDR2 sequence of SEQ ID NO: 2, and a VH-CDR3 sequence of SEQ ID NO: 3, and (b) the VL comprises a VL-CDR1 sequence of SEQ ID NO: 4, a V1-CDR2 sequence of SEQ ID NO: 5, and a VL-CDR3 sequence of SEQ ID NO: 6, wherein the at least one type of anti-CD3 multi-specific antibody is an immunoglobulin comprising two heavy chains and two light chains, wherein each of the light chains is fused to a single chain variable fragment (scFv), and wherein the ex vivo armed T cell is or has been cryopreserved. These deficiencies are remedied by Chang et al., Cheung et al., and Carter et al.
Chang et al. teach an anti-CD3 scFv that comprises the VH of SEQ ID NO: 96, which comprises the HCDRs of the instant SEQ ID NO(s): 1-3, respectively, and the VL of SEQ ID NO: 98, which comprises the LCDRs of the instant SEQ ID NO(s): 4-6, respectively. See [0232].
Cheung et al. teach a multi-specific antibody format that is an immunoglobulin comprising two heavy chains and two light chains, wherein each light chain is fused to an scFv that is specific for CD3, see Figure 1A.
Carter et al. teach that T cells that have been modified to target a protein of interest may be cryopreserved such that said T cells remain viable upon thawing, and Carter et al. teach that T cells “can be cryopreserved by methods known in the art to provide a permanent source of such T-cells for the future treatment of patients…” See [0117]. Based upon the teachings of Carter et al., one of ordinary skill in the art would reason that T cells may be cryopreserved such that they remain viable after thawing. Furthermore cryopreservation techniques provide a permanent source of T cells for clinical applications.
One of ordinary skill in the art would have been motivated with a reasonable expectation of success at the effective filing date of the invention to combine the teachings of Park et al., Chang et al., Cheung et al., and Carter et al. to develop an ex vivo armed T cell that is coated or complexed with an effective arming dose of at least one type of anti-CD3 multi-specific antibody, wherein the at least one type of anti-CD3/anti-GD2 multi-specific antibody includes a CD3 binding domain comprising a heavy chain immunoglobulin variable domain (VH) and a light chain immunoglobulin variable domain (VL), wherein (a) the VH comprises a VH-CDR1 sequence of SEQ ID NO: 1, a VH-CDR2 sequence of SEQ ID NO: 2, and a VH-CDR3 sequence of SEQ ID NO: 3, and (b) the VL comprises a VL-CDR1 sequence of SEQ ID NO: 4, a V1-CDR2 sequence of SEQ ID NO: 5, and a VL-CDR3 sequence of SEQ ID NO: 6, wherein the at least one type of anti-CD3 multi-specific antibody is an immunoglobulin comprising two heavy chains and two light chains, wherein each of the light chains is fused to a single chain variable fragment (scFv), and wherein the ex vivo armed T cell is or has been cryopreserved. One of ordinary skill in the art would have been motivated to do so, because Park et al. teach an ex vivo armed T cell that is coated or complexed with an effective arming dose of at least one type of anti-CD3/anti-GD2 multi-specific antibody, wherein the at least one type of anti-CD3 multi-specific antibody includes a CD3 binding domain comprising a heavy chain immunoglobulin variable domain (VH) and a light chain immunoglobulin variable domain (VL). Furthermore in view of Chang et al., one of ordinary skill in the art would have been motivated at the effective filing date of the invention to prepare an ex vivo armed T cell that expresses an anti-CD3/anti-GD2 multi-specific antibody that comprises an anti-CD3 scFv that comprises the VH of SEQ ID NO: 96, which comprises the HCDRs of the instant SEQ ID NO(s): 1-3, respectively, and the VL of SEQ ID NO: 98, which comprises the LCDRs of the instant SEQ ID NO(s): 4-6, respectively, because there would have been a reasonable expectation that said ex vivo armed T cell is effective in treating GD2-expressing cancers.
Additionally in view of the teachings of Cheung et al., one of ordinary skill in the art would have been motivated at the effective filing date of the invention to modify the invention of Park et al. and Chang et al. to comprise an ex vivo armed T cell that expresses an anti-CD3/anti-GD2 multi-specific antibody that is an immunoglobulin comprising two heavy chains and two light chains, wherein each light chain is fused to an scFv that is specific for CD3, because there would have been a reasonable expectation that said ex vivo armed T cell is effective in treating GD2-expressing cancers.
Lastly one of ordinary skill in the art would have been motivated at the effective filing date of the invention to prepare a cryopreserved ex vivo armed T cell, because based upon the teachings of Carter et al., one of ordinary skill in the art would reason that T cells may be cryopreserved such that they remain viable after thawing. Furthermore cryopreservation techniques provide a permanent source of T cells for clinical applications.
The invention of Park et al., Chang et al., Cheung et al., and Carter et al. meets the limitations of claims 1, 2, and 9.
With respect to claim 10, as indicted above, Cheung et al. teach a multi-specific antibody format that is an immunoglobulin comprising two heavy chains and two light chains, wherein each light chain is fused to an scFv that is specific for CD3.
Therefore the invention as a whole was prima facie obvious to one of ordinary skill in the art at the effective filing date of the invention, as evidenced by the references.
Claims 1, 2, 9, and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Cheung et al. (US PG PUB 2020/0199248, publication date: 06/25/2025, in IDS from 01/27/2023).
Cheung et al. teach a multi-specific antibody format that is an immunoglobulin comprising two heavy chains and two light chains, wherein each light chain is fused to an scFv that is specific for CD3, see Figure 1A. At column 9, Cheung et al. teach that “[p]rovided herein are bispecific binding molecules that bind to both HER2 and CD3. Also provided herein are isolated nucleic acids (polynucleotides), such as complementary DNA (cDNA), encoding such bispecific binding molecules or fragments thereof. Further provided are vectors (e.g., expression vectors) and cells (e.g., ex vivo cells) comprising nucleic acids (polynucleotides) or vectors (e.g., expression vectors) encoding such bispecific binding molecules or fragments thereof. Also provided herein are methods of making such bispecific binding molecules, cells, and vectors. Also provided herein are T cells bound to bispecific binding molecules provided herein. Also provided herein are methods of binding such bispecific binding molecules to T cells. In other embodiments, provided herein are methods and uses for treating HER2-positive cancers using the bispecific binding molecules, nucleic acids, vectors, and/or T cells described herein.” It is further noted that SEQ ID NO: 19 of Cheung et al. comprises the HCDRs of the instant SEQ ID NO(s): 1-3, respectively, and the LCDRs of the instant SEQ ID NO(s): 4-6, respectively. Column 67 of Cheung et al. teaches the cryopreservation of T cells.
Based upon these teachings, one of ordinary skill in the art would have been motivated to prepare an ex vivo armed T cell that is coated or complexed with an effective arming dose of at least one type of anti-CD3 multi-specific antibody, wherein the at least one type of anti-CD3 multi-specific antibody includes a CD3 binding domain comprising a heavy chain immunoglobulin variable domain (VH) and a light chain immunoglobulin variable domain (VL), wherein (a) the VH comprises a VH-CDR1 sequence of SEQ ID NO: 1, a VH-CDR2 sequence of SEQ ID NO: 2, and a VH-CDR3 sequence of SEQ ID NO: 3, and (b) the VL comprises a VL-CDR1 sequence of SEQ ID NO: 4, a V1-CDR2 sequence of SEQ ID NO: 5, and a VL-CDR3 sequence of SEQ ID NO: 6, wherein the at least one type of anti-CD3 multi-specific antibody is an immunoglobulin comprising two heavy chains and two light chains, wherein each of the light chains is fused to a single chain variable fragment (scFv), and wherein the ex vivo armed T cell is or has been cryopreserved. One of ordinary skill in the art would have been motivated to do so, because all elements of the invention are taught by Cheung et al. Furthermore there would have been a reasonable expectation that the invention rendered obvious by the teachings of Cheung et al. would be effective in the treatment of HER2-expressing cancers.
Therefore the invention as a whole was prima facie obvious to one of ordinary skill in the art at the effective filing date of the invention, as evidenced by Cheung et al.
Nonstatutory 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, 2, 9, and 10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, and 7 of U.S. Patent No. 11,987,642 in view of Carter et al. (US 2010/0105136, publication date: 04/29/2010).
The conflicting claim recite a composition comprising T cells bound to a bispecific binding molecule comprising a heavy chain monoclonal antibody that is an immunoglobulin that binds to HER2, comprising two identical heavy chains and two identical light chains, said light chains being a first light chain and a second light chain, wherein the first light chain is fused to a first single chain variable fragment (scFv), via a peptide linker, to create a first light chain fusion polypeptide, and wherein the second light chain is fused to a second scFv, via a peptide linker, to create a second light chain fusion polypeptide, wherein the first and second scFv (i) are identical, and (ii) bind to CD3, and wherein said scFv comprises SEQ ID NO: 19, which comprises the HCDRs of the instant SEQ ID NO(s): 1-3, respectively, and the LCDRs of the instant SEQ ID NO(s): 4-6, respectively.
Carter et al. teach that T cells that have been modified to target a protein of interest may be cryopreserved such that said T cells remain viable upon thawing, and Carter et al. teach that T cells “can be cryopreserved by methods known in the art to provide a permanent source of such T-cells for the future treatment of patients…” See [0117].
One of ordinary skill in the art would have been motivated to modify the conflicting claims to recite the cryopreservation of T cells bound to a bispecific binding molecule, because based upon the teachings of Carter et al., one of ordinary skill in the art would reason that T cells may be cryopreserved such that they remain viable after thawing. Furthermore cryopreservation techniques provide a permanent source of T cells for clinical applications.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NELSON B MOSELEY II whose telephone number is (571)272-6221. The examiner can normally be reached on M-F, 9:00-6:00 EST.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis, can be reached at 571-270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/NELSON B MOSELEY II/Primary Examiner, Art Unit 1642
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