DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Application Status
The amended claims filed January 15, 2025 are acknowledged. Claims 8 and 15 are canceled. Claims 5, 7, 9-11, 13, and 16-17 are amended.
Claims 1-7, 9-14, and 16-17 are pending and under examination herein.
It is noted that a Power of Attorney is not on record for the instant application. The Applicant is encouraged to file a Power of Attorney in the event that the Examiner needs to communicate with an authorized representative for the Applicant during the prosecution of the case.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. This application claims the benefit of priority of European Patent Application No. 21189516.4 filed on August 3, 2021, and U.S. Provisional Patent Application No. 63/345,966 filed on May 26, 2022.
The subject matter of claims 1 and 4-5 is supported in full by the priority document filed August 3, 2021.
The subject matter of claims 2-3, 6-7, 9-14 and 16-17 is supported in full by the priority document filed May 26, 2022.
It is noted that the European Patent Application No. 21189516.4 recites “P90S, E91D, S92V, and S93P” instead of “P91S, E92D, S93V, and S94P” as presently claimed. The TCRα polypeptide sequences of SEQ ID NOs: 47, 111, 114, and 117-120 and the TCRβ polypeptide sequences of SEQ ID NOs: 112-113, 115-116, and 121-122 are found only in the U.S. Provisional Patent Application 63/345,966 filed on May 26, 2022.
Claim Objections
Claim 9 is objected to under 37 CFR 1.75(c) as being in improper form because a multiple dependent claim must refer back to an earlier claim in the alternative only. Claims 10-11 are objected to under 37 CFR 1.75(c) as being in improper form because a multiple dependent claim must refer back to an earlier claim in the alternative only and cannot refer back to another multiple dependent claim (i.e., claim 9). Claims 12-14 and 16-17 are objected to under 37 CFR 1.75(c) as being in improper form because a multiple dependent claim cannot refer back to another multiple dependent claim. See MPEP § 608.01(n).
Accordingly, claims 9-14 and 16-17 have not been further treated on the merits herein.
Specification
The disclosure is objected to because of the following informalities: The title contains a typographical error; “game” should instead recite “same”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
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.
Claims 1-7 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 1 recites that the claimed T cell receptor (TCR) comprises a human TCRα polypeptide and a human TCRβ polypeptide (in lines 1-2), but later recites that the TCRα polypeptide comprises a chimeric human and murine TCRα polypeptide and that the TCRβ polypeptide comprises a chimeric human and murine TCRβ polypeptide (in (ii), lines 9-11). This renders the intended claim scope indefinite because it is unclear how the TCRα and TCRβ polypeptides comprised in the claimed TCR can simultaneously be fully human (as set forth at the beginning of the claim) while also being chimeric polypeptides that are not fully human (as set forth in (ii) in lines 9-11).
Claims 4-7, which depend from claim 1 and do not remedy this deficiency, are similarly rejected.
Claims 2 and 5 recite an embodiment in which the claimed T cell receptor (TCR) comprises a TCRβ polypeptide comprising an “E/V136A” amino acid substitution relative to the TCRβ polypeptide set forth in SEQ ID NO: 12. The claim language is indefinite because the reference sequence of SEQ ID NO: 12 comprises only a “V” at the cited residue, and it is unclear how the residue can contain two alternative residues (“E” or “V”) at the same position (position 136) in the wild-type condition.
Claims 3 and 6-7 depend from claim 2 and are similarly rejected.
Claim Rejections - 35 USC § 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.
Claim 1 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the 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. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991).
MPEP § 2163 states that 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, or it may be satisfied by the 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. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). “[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. For example, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875 (Fed. Cir. 2011).
The claimed invention. The nature and scope of the claimed invention at issue is a T cell receptor (TCR) comprising a human TCRα polypeptide and a human TCRβ polypeptide as set forth in claim 1, wherein said TCRα and TCRβ polypeptides “comprise amino acid modifications enabling presentation of said TCR as a TCR complex on a surface of a T cell expressing same”, wherein “said modifications comprise … (ii) said TCR alpha polypeptide and said TCR β polypeptide comprise a chimeric human and murine TCR alpha polypeptide and a chimeric human and murine TCR beta polypeptide” [sic]. (By the recitation of “or” in line 8, only one of (i) or (ii) is required to meet the limitations of the claim.) Claim 1 fails to satisfy the written description requirement because the recitation that “said TCR alpha polypeptide and said TCR β polypeptide comprise a chimeric human and murine TCR alpha polypeptide and a chimeric human and murine TCR beta polypeptide” does not provide sufficient structural information regarding the modifications that do confer the ability of the TCR to present as a TCR complex on the surface of a T cell expressing the same. As recognized by the state of the art below, not all murine-derived modifications to a human TCRα or TCRβ constant chain would be expected to be involved in the functional activity required by the claim.
State of the prior art. Chandran (Immunological Reviews (2019) 290(1): 127-147; cited in IDS) teaches that TCRs are heterodimers comprised most commonly of an α chain and a β chain, each containing a variable antigen-binding domain, an invariant extracellular constant region, and a transmembrane domain, which become covalently linked through a single disulfide bond facilitated by conserved cysteine residues located in the TCRα and TCRβ constant regions (e.g., Section 2.2). Chandran further teaches that adoptive transfer of exogenous TCR genes can contribute to the formation of mispaired TCRα/TCRβ heterodimer pairs, leading to safety and functional concerns (e.g., Section 3.1). Chandran discloses, “To minimize mispairing between the exogenous and endogenous TCR chains, hybrid TCRs can be created through genetic modifications to the extracellular constant chains. TCR murinization is the substitution of all or selected murine residues in place of the human sequence in the TCR constant regions. Murinized TCR chains preferentially pair and form more stable complexes with CD3ζ. Together, these properties result in higher exogenous TCR surface expression, increased functional avidity, and enhanced antigen-specific effector functions compared with a fully human receptor. … A second extracellular strategy to reduce TCR mispairing is the introduction of two complementary cysteine residues in the α and β constant regions to promote formation of a second interchain disulfide bond. Similar to murinization and domain swapping, this modification results in enhanced pairing of exogenous TCR chains. Finally, modifying the hydrophobicity of the TCRα TM region by substitution of three aliphatic residues in place of naturally occurring positively charged residues can also stabilize TCR surface expression” (Section 3.2).
Bialer (The Journal of Immunology (2010) 184(11): 6232-6241; cited in IDS) teaches that the primary structure of murine and human TCRα/TCRβ constant regions share 64.3% and 78.5% sequence identity, respectively (e.g., Results; Figure 1). Sommermeyer (The Journal of Immunology (2010) 184(11): 6223-6231; cited in IDS) investigated murinizing amino acid substitutions to human TCRs that improve their surface expression (e.g., Abstract). Sommermeyer identified four residues in the murine TCRα constant region (S91, D92, V93, and P94) which can be substituted at the corresponding human TCRα residues (i.e., P91S, E92D, S93V, and S94P in human TCRα) and five residues in the murine TCRβ constant region (K18, A22, I133, A136, and H139) which can be substituted at the corresponding human TCRβ residues (i.e., E18K, S22A, F133I, E136A, and Q139H in human TCRβ) to confer enhanced surface expression (e.g., Abstract; Results; Figures 3-4). The murinizing mutations of H23N and T24K in the human TCRα constant chain had negligible effect (e.g., Results).
Cohen (Cancer Research (2007) 67(8): 3898-3903; cited in IDS) further teaches that human, humanized, and murine TCRs expressed on the surface of human lymphocytes are more highly expressed when the amino acid substitution of T48C is incorporated into the TCRα constant region and the amino acid substitution of S57C is incorporated into the TCRβ constant region due to the preferential pairing of cysteine-modified receptor chains resulting from the additional disulfide bond (e.g., Abstract). As illustrated by Bialer at Figure 1, threonine (T) is the wild-type residue at position 48 in TCRα and serine (S) is the wild-type residue at position 57 in TCRβ in both the mouse and human TCRα and TCRβ constant regions.
Haga-Friedman (The Journal of Immunology (2012) 188(11): 5538-5546; cited in IDS) determined whether replacement of nonionizable transmembrane domain residues in the TCRα/TCRβ constant region with hydrophobic residues, while preserving the basic residues (R and K) responsible for interacting with the CD3 components, could compensate for lack of TCR chain stability and increase their surface expression and function (e.g., Abstract; Introduction; Results; Figure 1). Haga-Friedman observed that the TCRα constant region “LVL” mutations corresponding to S116L, G119V, and F120L significantly improved surface expression (e.g., Results; Figure 2C). Based on the teachings of Bialer, the human TCRα constant chain comprises S, G, and F as the wild-type residues at positions 116, 119, and 120, respectively, while the murine TCRα constant chain comprises S, G, and L at these same positions (Figure 1).
Scope of species disclosed in original specification. The working examples describe the generation of exemplary TCR constructs wherein (i) the TCRα constant region was modified with the mutations of (a) S116L, G119V, and F120L (“LVL”), (b) T48C, and/or (c) P91S, E92D, S93V, and S94P; and (ii) the TCRβ constant region was modified with the mutations of (a) S57C and/or (b) E18K, S22A, F133I, E136A, and Q139H; among others (e.g., Materials and Methods at page 54; Example 1), also illustrated in Figures 2A-2B and Table 1 (pages 57-58). The constructs comprise the amino acid sequences set forth in SEQ ID NOs: 2-3 and 26-32, 46-52, 57, 59, 61-69, 81, 83, 109, 123, 125 and 127 (e.g., Example 1). The examples disclose that inclusion of the TCRα mutation T48C and TCRβ mutation S57C was required to elicit expression of the truncated TCRα/β chains on the T cell surface, and that the addition of the LVL mutations further enhanced surface expression (e.g., Example 1 at page 56; Figures 3-4, Drawings). The examples further disclose that “minimal murine” (mm) mutations of P91S, E92D, S93V, and S94P in the TCRα chain and of E18K, S22A, F133I, E/V136A, and Q139H in the TCRβ chain also resulted in presentation of the truncated TCR complex on the T cell surface, which was further enhanced by the addition of the LVL modifications (e.g., Example 1 at pages 56-57; Figure 7, Drawings).
MPEP § 2163 states that 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 absence of a representative number of species, the written description requirement for a claimed genus may be satisfied 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. While eight exemplary constructs are summarized in Table 1, only the six comprising the “mmTRAC1”/”mmTRBC1” mutations and/or the TCRα LVL mutation (specifically, F120L) can be considered as chimeric TCR polypeptides comprising a combination of human and murine sequences. As also set forth in the prior art, the specific murinizing mutations of P91S, E92D, S93V, and S94P in the TCRα chain and of E18K, S22A, F133I, E/V136A, and Q139H in the TCRβ chain were specifically responsible for conferring enhanced TCRα/β surface expression. Not all murinizing mutations would be expected to contribute to or enhance surface expression of human TCRα/β chains.
Conclusion. For all of the reasons presented above, one of skill in the art would not know which of the countless other chimeric human/murine TCRα and TCRβ polypeptides encompassed by the highly general structural requirements of the claims would also possess the required functional activity of enabling presentation of the claimed TCR polypeptide on the surface of a T cell. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, the Applicant did not possess the full genus as broadly claimed at the time the application was filed.
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.
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.
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.
Claims 1-7 are rejected under 35 U.S.C. 103 as being unpatentable over Takayanagi (US 2022/0062341 A1; earliest priority date: December 26, 2018) in view of Ellinger (US 2023/0159612 A1; earliest priority date: March 27, 2019), Sommermeyer (The Journal of Immunology (2010) 184(11): 6223-6231; supra), and Haga-Friedman (The Journal of Immunology (2012) 188(11): 5538-5546; supra).
Takayanagi teaches that tissue injury caused by potent alloreaction from TCRα/TCRβ heterodimer expression by non-autologous T cells is a known problem in the field of non-autologous T cell therapy (¶ 0005). Although TCR gene knockdown or knockout has been used to solve this problem, Takayanagi notes, “When the TCR gene is knocked down or knocked out, however, the CD3 subunits are no longer held on the surface of cell membrane, and thus the proliferative signal and the survival signal through the TCR/CD3 complex is not input. This means, for example, that a CD3 agonist antibody or the like used for amplifying a donor-derived T cell preparation ex vivo does not function anymore, which is a problem in efficient production and formulation of a cellular medicine comprising non-autologous T cells” (¶ 0016).
To address this issue and to prevent the allorecognition response by non-autologous T cells, Takayanagi sets forth modified TCRs that do not cause antigen responsiveness and which are capable of holding CD3 subunits on a cell membrane and mediating CD3 signal transduction, wherein the modified TCR comprises (i) a first polypeptide which comprises a TCRα constant region and does not comprise a TCRα variable region and (ii) a second polypeptide which comprises a TCRβ constant region and does not comprise a TCRβ variable region (e.g., Abstract; ¶ 0016-0024; claim 1), pertinent to claims 1 and 2.
However, Takayanagi does not expressly disclose that the TCRα polypeptides of the invention comprise the amino acid substitutions of P91S, E92D, S93V, S94P, S116L, G119V, and F120L (relative to instant SEQ ID NO: 9), and that the TCRβ polypeptides of the invention comprise the amino acid substitutions of E18K, S22A, F133I, V136A, and Q139H (relative to instant SEQ ID NO: 12).
Ellinger teaches that mispairing between endogenous and exogenous TCR chains can lead to unpredictable TCR specificity and risk for cross-reactivity (e.g., ¶ 0114). Ellinger further teaches that mispairing of TCR sequences may be avoided by modifying recombinant TCR sequences to contain minimal murinized Cα and Cβ regions, which has been shown to efficiently enhance correct pairing of several different transduced TCR chains and to improve cell surface expression of TCRs in host cells (e.g., ¶ 0114). Ellinger proposes that “it is thought that murinized TCRs associate more effectively with CD3 co-receptors; and/or that preferentially pair with each other and are less prone to form mixed TCRs on human T cells genetically modified ex vivo to express the TCRs of desired antigenic specificity, but still retaining and expressing their ‘original’ TCRs” (¶ 0114). In particularly preferred embodiments, Ellinger states that “the recombinant TCR sequence is modified to contain minimal murinized Cα and Cβ regions and hydrophobic amino acid mutations in the Cα transmembrane domain. In particular embodiments, these TCRs have increased expression and functional avidity compared to TCRs that are not minimally murinized and do not contain hydrophobic mutations in the Cα transmembrane region” (¶ 0086).
Ellinger teaches exemplary TCRα constructs comprising the amino acid sequences of SEQ ID NOs: 114, 108, 116, and 110 (e.g., ¶ 0014-0016, 0026, 0114-0118, 0232-0236, 0283-0294), which comprise the TCRα constant chain having the amino acid sequence of instant SEQ ID NO: 119 and the amino acid modifications corresponding to P91S, E92D, S93V, and S94P, S116L, G119V, and F120L relative to instant SEQ ID NO: 9, relevant to claims 1-7. Ellinger further teaches exemplary TCRβ constructs comprising the amino acid sequences of SEQ ID NOs: 31, 103, 11, 116, and 104 (e.g., ¶ 0014-0016, 0116, 0283-0294), which comprise the TCRβ constant chain having the amino acid sequence of instant SEQ ID NO: 112 and the amino acid modifications corresponding to E18K, S22A, F133I, V136A, and Q139H relative to instant SEQ ID NO: 12, further relevant to claims 5 and 7.
As previously set forth in the 35 U.S.C. § 112(a) rejection above, Sommermeyer describes murinizing amino acid substitutions to human TCRs that improve their surface expression (e.g., Abstract). Sommermeyer identified four residues in the murine TCRα constant region (S91, D92, V93, and P94) which can be substituted at the corresponding human TCRα residues (i.e., P91S, E92D, S93V, and S94P in human TCRα) and five residues in the murine TCRβ constant region (K18, A22, I133, A136, and H139) which can be substituted at the corresponding human TCRβ residues (i.e., E18K, S22A, F133I, E136A, and Q139H in human TCRβ) to confer enhanced surface expression (e.g., Abstract; Results; Figures 3-4).
As previously set forth in the 35 U.S.C. § 112(a) rejection above, Haga-Friedman investigated whether replacement of nonionizable transmembrane domain residues in the TCRα/TCRβ constant region with hydrophobic residues, while preserving the basic residues (R and K) responsible for interacting with the CD3 components, could compensate for lack of TCR chain stability and increase their surface expression and function (e.g., Abstract; Introduction; Results; Figure 1). Haga-Friedman observed that the TCRα constant region “LVL” mutations corresponding to S116L, G119V, and F120L significantly improved surface expression (e.g., Results; Figure 2C).
Taken together, it would have been obvious to one of ordinary skill in the art, before the filing date of the instantly claimed invention, to substitute into the modified TCRs taught by Takayanagi a chimeric TCRα constant region polypeptide that comprises the substitutions of P91S, E92D, S93V, S94P, S116V, G119V, and F120L (relative to instant SEQ ID NO: 9), and a chimeric TCRβ constant region polypeptide that comprises the substitutions of E18K, S22A, F133I, E136A, and Q139H (relative to instant SEQ ID NO: 12) based on the further teachings of Ellinger, Sommermeyer, and Haga-Friedman. The skilled artisan would have been motivated to do so because Ellinger and Sommermeyer set forth that minimal murinized Cα and Cβ regions have been shown to efficiently enhance correct pairing of several different transduced TCR chains and to improve cell surface expression of TCRs in host cells. Furthermore, Ellinger and Haga-Friedman set forth that hydrophobic mutations in the TCRα constant chain also enhance surface expression of TCRs. There would have been a reasonable expectation of success because one of ordinary skill in the art would have recognized that the murinizing mutations of P91S, E92D, S93V, and S94P in the TCRα constant region and E18K, S22A, F133I, E136A, and Q139H in the TCRβ constant region have been specifically demonstrated by Sommermeyer to improve surface expression of TCRs, and because the LVL mutations of S116L, G119V, and F120L have been specifically demonstrated by Haga-Friedman to also promote increased surface expression of TCRs. Furthermore, Ellinger provides exemplary constructs in which these mutations have been introduced.
Conclusion
No claims are allowed.
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/ELIZABETH A SHUPE/Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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