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
Election Response
The Election filed 11/10/2025, in response to the Office Action of 8/11/2025, is acknowledged and has been entered. Applicants elected without traverse Group III (claims 12, 16-27, 31-41), and the species VH comprising HCDR1 having SEQ ID NO: 79, a HCDR2 having SEQ ID NO: 56, and a HCDR3 having SEQ ID NO: 10; and a VL comprising a LCDR1 having SEQ ID NO: 102, a LCDR2 having sequence A9 (of Figure 1), and a LCDR3 having SEQ ID NO: 33.
Claims 12, 16-27, and 31-41 are pending and are currently under prosecution.
Specification/Drawings
Nucleotide and/or Amino Acid Sequence Disclosures
Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures
37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted:
1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying:
a. the name of the XML file
b. the date of creation; and
c. the size of the XML file in bytes; or
2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying:
a. the name of the XML file;
b. the date of creation; and
c. the size of the XML file in bytes.
SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS: This application contains sequence disclosures in accordance with the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.831(a) and 1.831(b). However, this application fails to comply with the requirements of 37 CFR 1.831-1.834. The Examiner has noted that Figure 5 does not have SEQ ID Nos for the recited sequences.
Applicant must provide:
• A replacement “Sequence Listing XML” part of the disclosure, as described above in item 1. or 2., as well as
• A statement that identifies the location of all additions, deletions, or replacements of sequence information in the “Sequence Listing XML” as required by 1.835(b)(3);
• A statement that indicates support for the amendment in the application, as filed, as required by 37 CFR 1.835(b)(4);
• A statement that the “Sequence Listing XML” includes no new matter in accordance with 1.835(b)(5); and
• A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation by reference paragraph as required by 37 CFR 1.835(b)(2), consisting of:
o A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
o A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Interpretation
Claim 12 recites: “"An ex vivo method of modulating gamma variable 4 (Vγ4) T cells comprising to a cell population comprising Vγ4 T-cells an anti-Vγ4 antibody or fragment thereof, comprising (a) a VH comprising a HCDR1 having SEQ ID NO: 79, a HCDR2 HAVING seq id no: 56, and a HCDR3 having SEQ ID NO: 10; and (b) a VL comprising a LCDR1 having SEQ ID NO: 102, a LCDR2 having SEQUENCE A9 (of FIGURE 1) and a LCDR3 having SEQ ID NO: 33.
Examiner has interpreted the claim as the following:
“SEQUENCE A9” as “EVT” as shown in Figure 1
the term “modulating” as increasing or decreasing gamma variable 4 (Vγ4) T cells, and as disclosed in the instant specification and is supported in Examples of the specification.
Modulation of Vγ4 T cells may include: [pg 20-21 of instant specification]
expansion of the Vγ4 T cells, e.g. by selectively increasing the number of Vγ4 T cells or promotion of survival of Vγ4 T cells;
stimulation of the Vγ4 T cells, e.g. by increasing Vγ4 T cell potency, i.e. increasing target cell killing;
prevention of Vγ4 T cell exhaustion, e.g. by increasing persistence of the Vγ4 T cells; degranulation of Vγ4 T cells;
immunosuppression of the Vγ4 T cells, e.g. by downregulation of Vγ4 TCR cell surface expression, i.e. by causing Vγ4 TCR internalisation or reduced expression of Vγ4 TCR protein, or blocking the Vγ4 TCR from binding;
reducing Vγ4 T cell number, e.g. by inhibition of Vγ4 T cell proliferation or by inducing Vγ4 T cell death (i.e. killing Vγ4 T cells).
Claim Objections
Claim 12 is objected to because of the following informalities: Applicant recites LCDR2 having SEQUENCE A9 of Figure 1. Examiner suggests the claim is amended to incorporate the SEQUENCE A9, that is “EVT” as noted in Figure 1. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 31-40 are 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. This is a WRITTEN DESCRIPTION rejection.
Dependent claims 31-40 recite partial structure of the anti-Vγ4 antibody:
Claim 31 recites: The method as defined in claim 12, wherein:
the VH comprises an amino acid sequence having at least 95% sequence identity with SEQ ID NO: 125;
the VL comprises an amino acid sequence having at least 95% sequence identity with SEQ ID NO: 148 or 269 or
both (i) and (ii)
Claim 32 recites: The method as defined in claim 12, wherein:
the VH comprises an amino acid sequence having SEQ ID NO: 125;
the VL comprises an amino acid sequence having SEQ ID NO: 148 or 269 or
both (i) and (ii)
Claim 33 recites: The method as defined in claim 12, wherein:
the VH comprises an amino acid sequence having SEQ ID NO: 125;
the VL comprises an amino acid sequence having SEQ ID NO: 148 or
both (i) and (ii)
Claim 34 recites: The method as defined in claim 12, wherein:
the VH comprises an amino acid sequence having SEQ ID NO: 125;
the VL comprises an amino acid sequence having SEQ ID NO: 269 or
both (i) and (ii)
Claim 35 recites: The method as defined in claim 12, wherein:
a heavy chain amino acid sequence having at least 95% sequence identity with SEQ ID NO: 292;
a light chain amino acid sequence having at least 95% sequence identity with SEQ ID NO: 315;
both (i) and (ii)
Claim 36 recites: The method as defined in claim 12, wherein:
a heavy chain amino acid sequence having SEQ ID NO: 292;
a light chain amino acid sequence having SEQ ID NO: 315;
both (i) and (ii)
Thus, claims 31-34 recite partial structure of the antibody, that is that the antibody may comprise a VH or a VL comprising the instantly claimed sequences, and claims 35-36 recite that the antibody may comprise a heavy chain amino acid or a light chain amino acid sequence. Claims 37 and 39 recite that the antibody of claim 12 has 95% sequence identity with SEQ ID NO: 241 and 171. Thus, the claims encompass a genus of sequences having up to 5% sequence discrepancy from the disclosed SEQ ID Nos.
The instant specification discloses full and specific sequences of heavy chain and light chains that are used together [see at least pg 41]. However, does not disclose any examples that include either the heavy chain or light chain, and not disclose does not disclose any representative variants of the antibody with less than 100% SEQ ID Nos.
By the time of the filing of the instant application, it was well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33; (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4.
Antibody binding to the same antigen, or even the same epitope on that antigen, can be accomplished with an impressively wide variety of antibody structures, even when the antibodies are limited to those from a particular source (Gershoni et al., Epitope Mapping, Biodrugs 2007; 21 (3): 145-156 page 146 section 1.1). The skilled artisan therefore understood that antibodies from a variety of different sources may bind the same antigen and even mediate the same functional effects, but differ widely in the details of the structure of their antigen-binding sites.
Further, it is not possible to predict the amino acid sequence when an epitope is recited, because there are many different epitope arrangements, such as linear and discontinuous epitopes that is dictated by the unique interaction between an antibody and its cognate epitope (Blythe et al., Benchmarking B cell epitope prediction: Underperformance of existing methods, Protein Science (2005), 14:246–248 pg. 246) . 3D structural analyses of antibody-epitope binding highlighting that the deficiency in the ability to predict the structural features of an antibody when the epitope is disclosed (Schreiber et al.,3D-Epitope-Explorer (3DEX): Localization of Conformational Epitopes within Three-Dimensional Structures of Proteins, Wiley Interscience, 2005 42–44, 60596, page 879).
Furthermore, changes in amino acid structures can have impacts on antigen binding that are unpredictable. Rabia et al (Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility. Biochemical engineering journal, 137, 365–374, 2018) and Vajdos et al (Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. Journal of molecular biology, 320(2), 415–428, 2022) teaches that changes to CDRs are unpredictable in terms of affinity, specificity, and solubility, (see Rabia whole documents), and teaches that even minute changes to the CDR region can impact binding affinities. (see Figure 2, effects of CDR mutations on binding affinity), respectively. Rudikoff et al (Single amino acid substitution altering antigen-binding specificity. Proc Natl Acad Sci U S A. 1982 Mar;79(6):1979-83) teaches that single amino acid substitutions alter antigen-binding specificity. [Abstract] Lastly, Herold et al (Sci Rep. 2017 Sep 25;7(1):12276) teaches and demonstrates that single and double mutations in exemplary antibodies, and found that single point mutations in the VH CDR region can completely abolish antigen binding. [see pg 8]
The structure activity relationship of the CDR antigen binding region that recognizes anti-Vγ4 antibodies is not known and the binding epitopes cannot be predicted based on the antibody sequences.
To provide adequate written description and evidence of possession of the claimed composition antibody genus, the instant specification can structurally describe representative antibodies or antigen binding fragments, or describe structural features common to the members of the genus, which features constitute a substantial portion of the genus. Alternatively, the specification can show that the claimed invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics (see University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) and Enzo Biochem, Inc. V. Gen-Probe Inc.). A disclosure that does not adequately describe a product itself logically cannot adequately describe a method of using that product.
Although Applicants may argue that it is possible to screen for antibodies that function as claimed, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly, “[a]n adequate written description of a DNA … ‘requires a precise definition, such as by structure, formula, chemical name, or physical properties,’ not a mere wish or plan for obtaining the claimed chemical invention.” 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” Knowledge of screening methods provides no information about the structure of any future antibodies yet to be discovered that may function as claimed.
Applicants have not established any reasonable structure-function correlation with regards to the sequences of the claimed antibody that can be altered and still maintain function. Therefore, one could not readily envision members of the broadly claimed genus.
Given the lack of representative examples to support the full scope of the claimed antibodies, and lack of reasonable structure-function correlation with regards to the unknown sequences in the variable domains or CDRs of the antibodies that function as claimed, the present claims lack adequate written description. Thus, the specification does not provide an adequate written description of antibodies that is required to practice the claimed invention. Since the specification fails to adequately describe the product to which the claimed method uses, it also fails to adequately describe the method.
Examiner’s Suggestion: Amend the claims to include the full structure, that is both the VH and VL sequences (claims 31-34), the heavy and light chain amino acid sequences (claims 35-36), and the full structure of the amino acid sequences as noted in claims 37-39.
Claims 31-40 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for the method comprising administering an antibody with both the heavy and light chains, does not reasonably provide enablement for the method comprising administering a heavy chain or a light chain of the claimed antibody. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to practice the invention commensurate in scope with these claims.
BREADTH OF THE CLAIMS: Dependent claims 31-40 recite partial structure of the anti-Vγ4 antibody and recite that the antibody can include either a heavy chain or a light chain.
PRESENCE OR ABSENCE OF EXAMPLES: The instant specification discloses the uses and production of antibodies with both a heavy chain and light chains. There is no example of use of just an antibody with either the light chain or the heavy chain.
STATE OF THE ART: It is well known in the art that full structures of antibodies are needed for function and that any changes in amino acid structures can have impacts on antigen binding that are unpredictable. Rabia et al (Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility. Biochemical engineering journal, 137, 365–374, 2018) and Vajdos et al (Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. Journal of molecular biology, 320(2), 415–428, 2022) both teach that changes to the structure unpredictable in terms of affinity, specificity, and solubility, (see Rabia whole documents), and teaches that even minute changes to the CDR region can impact binding affinities. (see Figure 2, effects of CDR mutations on binding affinity), respectively. Thus, without knowing the complete structure of the antibody, it does not provide any support that the antibody will be have the same function properties.
PREDICITABILITY: The specification lacks the critical steps necessary in presenting some type of predictable response in a population of hosts deemed necessary to modulate the T-cells with an antibody that just comprises one chain, either the heavy or light chain. There is no evidence in the instant application or the art that as noted in the prior that would function as claimed. Thus, considering the high level of skill in the art, the state of the art, the level of predictability, and the guidance and examples provided, the experimentation required to enable the full scope of the claimed invention would not be reasonable.
QUANTITY OF EXPERIMENTATION: Undue experimentation would be required to determine claimed agent is administered to which population of subjects could function as claimed. MPEP 2164.01 recites that “The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue. In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976)”. The experimentation needed to practice this method is undue and unreasonable as it requires determining whether the claimed antibody can be used as claimed. A person skilled in the art will not be able to use the invention without undue experimentation. (In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988))
Accordingly, the instant claims do not comply with the enablement requirement of §112, since to practice the invention claimed in the patent a person of ordinary skill in the art would have to engage in undue experimentation, with no assurance of success.
Examiner’s suggestion: Amend the claims to recite the full structure, that is both the VH and VL and the heavy and light chain sequence.
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 12, 16-27, and 31-41 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 12 is indefinite in the use of the expression in parenthesis “(of Figure 1)” in that it is not clear whether this recitation is intended to be part of the claim or not.
Claim(s) 12 is rejected for making reference to tables within the specification and/or figure(s). Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table “is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim.” See MPEP 2173.05(s).
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.
Claim 12, 16-19, 25-27, and 31-40 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 12-15, 17-18, 20-23 and 30-34 of copending Application No. 17/801,786 (reference application, recently allowed 8/4/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because the co-pending application recites an anti-gamma variable 4 antibody comprising the instantly claimed sequences (see sequence alignments below). The co-pending application also recites a method of expanding a Vγ4+ T-cell (claim 32), a method of detecting a Vγ4+ T-cell (claim 33), which falls under the definition of “modulating a Vγ4 T-cell” as noted in instantly claimed 17. The co-pending application also recites the limitations of instantly claimed 16, wherein the anti- Vγ4 fragment thereof is: (i) an scFv or a full length antibody; and/or (ii) a human antibody of fragment thereof.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
SEQUENCE ALIGNMENTS
VH CDR1-3: SEQ ID Nos: 79-56-10
RESULT 1
US-17-801-786-125
Sequence 125, US/17801786
Publication No. US20230090901A1
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 125
LENGTH: 117
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: TRGV4 full heavy variable sequence G4_12
Query Match 79.8%; Score 101.3; Length 117;
Best Local Similarity 29.6%;
Matches 24; Conservative 0; Mismatches 0; Indels 57; Gaps 2;
Qy 1 GFTVSSNY-----------------IYSGGST---------------------------- 15
|||||||| |||||||
Db 26 GFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYADSVKGRFTISRHNSKNTLYLQMNSL 85
Qy 16 ------------VANGDFLDY 24
|||||||||
Db 86 RAEDTAVYYCARVANGDFLDY 106
VL CDR1-3: SEQ ID Nos: 102-EVT-33
RESULT 1
US-17-801-786-269
Sequence 269, US/17801786
Publication No. US20230090901A1
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 269
LENGTH: 108
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: TRGV4 full light variable sequence G4_12 no N-terminal AS
Query Match 75.4%; Score 77.7; Length 108;
Best Local Similarity 27.4%;
Matches 20; Conservative 0; Mismatches 0; Indels 53; Gaps 2;
Qy 1 SSDVGGYNF-----------------EVT------------------------------- 12
||||||||| |||
Db 26 SSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPSGVPDRFSGSKSGNTASLTISGLQAEDE 85
Qy 13 -----SSHASPRV 20
||||||||
Db 86 ADYYCSSHASPRV 98
SEQ ID NO: 125
RESULT 1
US-17-801-786-125
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 125, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 125
LENGTH: 117
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: TRGV4 full heavy variable sequence G4_12
Query Match 100.0%; Score 612; Length 117;
Best Local Similarity 100.0%;
Matches 117; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
Qy 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSS 117
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSS 117
SEQ ID NO: 148
RESULT 1
US-17-801-786-148
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 148, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 148
LENGTH: 110
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: TRGV4 full light variable sequence G4_12
Query Match 100.0%; Score 572; Length 110;
Best Local Similarity 100.0%;
Matches 110; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
Qy 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 110
||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 110
SEQ ID NO: 269
RESULT 1
US-17-801-786-269
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 269, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 269
LENGTH: 108
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: TRGV4 full light variable sequence G4_12 no N-terminal AS
Query Match 100.0%; Score 564; Length 108;
Best Local Similarity 100.0%;
Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPSGV 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPSGV 60
Qy 61 PDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 108
||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 PDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 108
SEQ ID NO: 292
RESULT 1
US-17-801-786-292
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 292, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 292
LENGTH: 447
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: G4_12 IgG1 antibody heavy chain sequence
Query Match 100.0%; Score 2379; Length 447;
Best Local Similarity 100.0%;
Matches 447; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
Qy 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSAST 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSAST 120
Qy 121 KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY 180
Qy 181 SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSV 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSV 240
Qy 241 FLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTY 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 FLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTY 300
Qy 301 RVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 RVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK 360
Qy 361 NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG 420
Qy 421 NVFSCSVMHEALHNHYTQKSLSLSPGK 447
|||||||||||||||||||||||||||
Db 421 NVFSCSVMHEALHNHYTQKSLSLSPGK 447
SEQ ID NO: 315
RESULT 1
US-17-801-786-315
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 315, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 315
LENGTH: 216
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: G4_12 IgG1 antibody light chain sequence
Query Match 100.0%; Score 1125; Length 216;
Best Local Similarity 100.0%;
Matches 216; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
Qy 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVLGQPAAAPSVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVLGQPAAAPSVT 120
Qy 121 LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASS 180
Qy 181 YLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS 216
||||||||||||||||||||||||||||||||||||
Db 181 YLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS 216
SEQ ID NO: 241
RESULT 1
US-17-801-786-241
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 241, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 241
LENGTH: 663
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: G4_12 IgG1 antibody sequence
Query Match 100.0%; Score 3504; Length 663;
Best Local Similarity 100.0%;
Matches 663; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKLMIYEVTNRPS 60
Qy 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVLGQPAAAPSVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVLGQPAAAPSVT 120
Qy 121 LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASS 180
Qy 181 YLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSEVQLLESGGGLVQPGGSLRLSCAA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSEVQLLESGGGLVQPGGSLRLSCAA 240
Qy 241 SGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYADSVKGRFTISRHNSKNTLYLQMNS 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 SGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYADSVKGRFTISRHNSKNTLYLQMNS 300
Qy 301 LRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGC 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 LRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGC 360
Qy 361 LVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 LVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH 420
Qy 421 KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVV 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVV 480
Qy 481 DVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 DVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS 540
Qy 541 NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESN 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESN 600
Qy 601 GQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLS 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 GQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLS 660
Qy 661 PGK 663
|||
Db 661 PGK 663
SEQ ID NO: 171
RESULT 1
US-17-801-786-171
(NOTE: this sequence has 1 duplicate in the database searched)
Sequence 171, US/17801786
GENERAL INFORMATION
APPLICANT: GammaDelta Therapeutics Limited
TITLE OF INVENTION: Novel Antibodies
FILE REFERENCE: T0833.70026US00
CURRENT APPLICATION NUMBER: US/17/801,786
CURRENT FILING DATE: 2022-08-23
PRIOR APPLICATION NUMBER: PCT/GB2021/050459
PRIOR FILING DATE: 2021-02-24
PRIOR APPLICATION NUMBER: GB 2002581.3
PRIOR FILING DATE: 2020-02-24
NUMBER OF SEQ ID NOS: 338
SEQ ID NO 171
LENGTH: 277
TYPE: PRT
ORGANISM: artificial sequence
FEATURE:
OTHER INFORMATION: scFv sequence G4_12
Query Match 100.0%; Score 1478; Length 277;
Best Local Similarity 100.0%;
Matches 277; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLLESGGGLVQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSGGSTYYA 60
Qy 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSGGG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 DSVKGRFTISRHNSKNTLYLQMNSLRAEDTAVYYCARVANGDFLDYWGRGTLVTVSSGGG 120
Qy 121 GSGGGGSGGGASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKL 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GSGGGGSGGGASQSVLTQPASVSGSPGQSITISCTGTSSDVGGYNFVSWYQQHPGKAPKL 180
Qy 181 MIYEVTNRPSGVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 MIYEVTNRPSGVPDRFSGSKSGNTASLTISGLQAEDEADYYCSSHASPRVFGTGTKVTVL 240
Qy 241 RTAAASAHHHHHHKLDYKDHDGDYKDHDIDYKDDDDK 277
|||||||||||||||||||||||||||||||||||||
Db 241 RTAAASAHHHHHHKLDYKDHDGDYKDHDIDYKDDDDK 277
Closest Prior Art
The closest prior art made of record is Langerak et al ("Immunophenotypic and immunogenotypic characteristics of TCRγδ⁺ T cell acute lymphoblastic leukemia," published February 5, 1999). Langerak teaches specific antibodies for the V₃₄ domains of TCR chain. Langerak also teaches testing an antibody panel including V₈₄ to study TCRyδ⁺ T-ALL in more detail (page 210). However, Langerak does not teach that the antibodies comprise the instantly claimed sequences.
Conclusion
Conclusion: Claim 12 is objected to. Claims 12, 16-27, and 31-41 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SARAH A ALSOMAIRY whose telephone number is (571)272-0027. The examiner can normally be reached Monday-Friday 7:30 AM to 5:30 PM.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory Emch can be reached at (571) 272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/SARAH A ALSOMAIRY/Examiner, Art Unit 1646
Prosecution Insights