Prosecution Insights
Last updated: April 19, 2026
Application No. 17/640,281

CHIMERIC ANTIGEN RECEPTORS AND RELATED METHODS AND COMPOSITIONS FOR THE TREATMENT OF CANCER

Non-Final OA §103
Filed
Mar 03, 2022
Examiner
SPENCE, JENNIFER SUZANNE
Art Unit
1633
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
The Regents of the University of California
OA Round
3 (Non-Final)
67%
Grant Probability
Favorable
3-4
OA Rounds
3y 10m
To Grant
99%
With Interview

Examiner Intelligence

Grants 67% — above average
67%
Career Allow Rate
71 granted / 106 resolved
+7.0% vs TC avg
Strong +45% interview lift
Without
With
+45.1%
Interview Lift
resolved cases with interview
Typical timeline
3y 10m
Avg Prosecution
63 currently pending
Career history
169
Total Applications
across all art units

Statute-Specific Performance

§101
4.6%
-35.4% vs TC avg
§103
42.1%
+2.1% vs TC avg
§102
16.0%
-24.0% vs TC avg
§112
23.4%
-16.6% vs TC avg
Black line = Tech Center average estimate • Based on career data from 106 resolved cases

Office Action

§103
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 . Continued Examination Under 37 CFR 1.114 A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 12/12/2025 has been entered. Claims 1, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, 72, and 75, of record 11/12/2025, are pending and subject to prosecution. Claims 1, 4, and 26-27 are amended. Claim 74 is cancelled. The amendment to the claims filed on 11/12/2025, does not comply with the requirements of 37 CFR 1.121(c) because the status listing for claim 75 is incorrect. Amendments to the claims filed on or after July 30, 2003 must comply with 37 CFR 1.121(c). The amendment under consideration herein fails to comply with 37 CFR 1.121 because the claim listing present claim 75 as “new” rather than “previously presented”. The amendment could be therefore considered non-responsive. In the interest of compact prosecution, the amendment at issue will not be considered non-responsive, however, any future responses failing to comply with 37 CFR 1.121 will be held non-responsive and will not be considered. Status of Prior Rejections/Response to Arguments RE: Rejection of claims 4-5 under 35 U.S.C. 112(b): The amendment to make claim 4 depend from claim 3 is effective to obviate the rejection. The rejection is withdrawn. RE: Rejection of claims 1, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, 72, and 74 under 35 U.S.C. 103 over Mujacic et al. (WO 2019113557 A1) in view of Balderes et al. (US 7951370 B2): RE: Rejection of claims 1, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, 72, and 74-75 are rejected under 35 U.S.C. 103 over Mujacic et al. (WO 2019113557 A1) in view of Balderes et al. (US 7951370 B2), further in view of Forman et al. (US 20160333108 A1): The cancellation of claim 74 renders the rejection thereto moot. The applicant asserts that amended claim 1, which now requires an extracellular spacer derived from an immunoglobulin-type hinge and having at least 120 amino acids for the CAR, as well as VH and VL regions having at least 90% identity to instant SEQ ID NOs 5 and 10, is not taught or suggested by the prior art (Applicant Remarks, page 6). The applicant asserts that Mujasic et al. teach CAR targets, spacers, and spacer lengths only generically and does not disclose a CAR comprising TYRP-1-specific scFvs or benefits associated with a long immunoglobulin spacer (Applicant Remarks, page 6-7). The applicant asserts that Forman et al. do not provide any reason to use the spacer sequence comprising SEQ ID NO 16 in the context of a TYRP-1-specific CAR (Applicant Remarks, page 7). The applicant also asserts unexpected results in the form of greater in vitro cytotoxicity and IFN-γ secretion across human and murine melanoma cell lines, as well as superior effects in patient-derived xenograft models (Applicant Remarks, page 7-8). The applicant’s arguments have been fully considered but are not found persuasive. The combined teachings of Mujasic et al. and Baldares et al. disclose every limitation of independent claim 1, and sufficient motivation exists for such a combination. Mujasic et al. teach that the antigen targeted by the CAR can be TYRP1 (See ¶0651); the idea of a TYRP1-specific CAR is not rendered less obvious by TYRP1 being one of a list of antigens. Mujasic et al. also teach that the CAR spacer can be long, about 229 amino acids or less (See ¶0685); All of the claimed components are taught by the prior art as being suitable for CAR construction. Additionally, simple substitution of known equivalents does not require any motivation to be provided by Forman et al., as there is no evidence that the substitution yields more than predictable results. See MPEP 2143(I)(B). With regard to applicant’s alleged later finding that spacer length is critical for CAR targeting of TYRP1, the examiner is not persuaded. The applicant asserts that the activity of the anti-TRYP1 CAR is dependent on a long immunoglobulin-derived spacer (Applicant Remarks, page 7-8), however, where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation (In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955); Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382; In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969)). See MPEP 2144.05(II)(A). Further regarding the assertion of unexpected results, Kokalaki generated and tested TYRP1-targeting CARs with spacers of different lengths in order to determine optimal CAR structure (See fig. 36). Cytotoxicity and IFN-γ production were highest for the two constructs having the longest spacers, one comprising the IgG CH2-CH3 domain and hinge region and the other comprising the IgM constant heavy domains CH2-CH3-CH4 (See page 125-126, 4.3.2.1 and fig. 38-39). Schroeder et al. teach that each constant domain consists of approximately 110-130 amino acids (See page S41, col. 2, 2), which would place the length of Kokalaki’s IgG and IgM spacers around 220-260 aa and 330-390 aa, respectively. In light of the teachings of Kokalaki, one of ordinary skill in the art could have reasonably expected to observe higher cytotoxic activity and cytokine secretion by using CARs having longer spacers to target TYRP-1. Further, in order to overcome a finding of obviousness, any evidence must be fully commensurate in scope with the claims. See MPEP 716.02(d). The scope of instant claim 1 encompasses considerably more constructs than those tested in the disclosure. No additional evidence is provided to indicate that any variants, in addition to those tested, would also yield enhanced results. The instant disclosure is insufficient to provide a structure-function relationship among species having extended spacers that would enable one of ordinary skill in the art to extrapolate such results to other CAR variants encompassed by the claims. The rejections are maintained. Maintained Rejections Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. 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, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, and 72 remain rejected under 35 U.S.C. 103 as being unpatentable over Mujacic et al. (WO 2019113557 A1), of record, in view of Balderes et al. (US 7951370 B2), of record. Regarding claims 1, 3, 26-27, 49, 54, and 64: Mujacic et al. teach methods for producing a population of T cells expressing a recombinant receptor, such as a CAR (which reads on “a chimeric polypeptide”) (See ¶0007, 0014, 0060, and 0089). Cells can be treated or contacted with a nucleic acid that encodes the receptor (See ¶0161, 0325, and 0330). The CAR can comprise an antigen-binding domain, a transmembrane domain, and an intracellular signaling domain (See ¶0060-0062). Mujacic et al. teach that the CAR can comprise a IgG4 hinge, an IgG4 hinge linked to CH2 and CH3 domains (which reads on “an IgG4-CH2CH3 hinge”), or an IgG4 hinge linked to a CH3 domain (which reads on “an IgG4-CH3 hinge”) and that that the hinge region (which reads on “extracellular spacer”) can be about 10-229 amino acids in length (which reads on “a length of at least 120 amino acids” and “between 200 and 300 amino acids in length”) (See ¶0684-0685). The antigen-binding domain can be an antibody or antibody fragment such as an scFv comprising VH and VL regions joined by a linker (See ¶0060, 0271, 0646, and 0662). The antigen binding domain can target TYRP-1 (See ¶0650-0651 and 0783). Mujacic et al. do not teach the antigen-binding domain as comprising specific sequences for targeting TYRP-1. Balderes et al. teach human antibodies specific for TYRP-1 (See Abstract). Balderes et al. teach a monoclonal antibody having a light chain comprising the sequence of instant SEQ ID NO 5 (See col. 3, lines 27-30; SEQ ID NO 32; and alignment below). The sequence taught by Balderes et al. also encompasses instant SEQ ID NOs 6 (RASQSVSSYLA), 7 (DASNRAT), and 8 (QQRSNWLMYT) (See col. 2, lines 43-58 and alignment below). PNG media_image1.png 176 581 media_image1.png Greyscale Balderes et al. teach the monoclonal antibody as having a heavy chain comprising the sequence of instant SEQ ID NO 10 (See col. 3, lines 27-30; SEQ ID NO 30; and alignment below). The sequence also encompasses instant SEQ ID NOs 11 (GYTFTSYAMN), 12 (WINTNTGNPTYAQGFTG), and 13 (RYSSSWYLDY) (See col. 2, lines 43-58 and alignment below). PNG media_image2.png 174 580 media_image2.png Greyscale It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the CAR of Mujacic et al. to comprise the sequences taught by Balderes et al. for targeting TYRP-1-expressing tumor cells. One would be motivated to make this modification because Balderes et al. teach these sequences as exemplary sequences for binding TYRP-1 (See col. 2, lines 43-58). There would be a reasonable expectation of success in doing so because the CAR of Mujacic et al. could be readily engineered to comprise the sequences taught by Balderes et al. Regarding claims 4-5: Following the discussion of claims 1, 3, 26-27, 49, 54, and 64, Mujacic et al. teach that the linker between VH and VL regions can be between about 5-50 amino acids in length (See ¶0662). An exemplary linker comprises 2-5 repeats of GGGGS (which reads on “a Whitlow linker, (G4S)n… wherein n is 1, 2, 3, 4, 5, or 6”) (See ¶0662). Where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists. See MPEP 2144.05(I). Regarding claims 11-12: Following the discussion of claims 1, 3, 26-27, 49, 54, and 64, Mujacic et al. teach that the transmembrane domain of the CAR can be derived from a TCR alpha or beta chain, CD28, CD3 epsilon, CD45, CD4, CD5, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, or CD154 (See ¶0690). Regarding claims 14 and 18-19: Following the discussion of claims 1, 3, 26-27, 49, 54, and 64, Mujacic et al. teach that the CAR can comprise a primary signaling sequence derived from CD3zeta and a signaling region and/or transmembrane portion of a costimulatory receptor such as CD28, 4-1BB, OX40, and ICOS (See ¶0696-0697). Regarding claims 23-24: Following the discussion of claims 1, 3, 26-27, 49, 54, and 64, Mujacic et al. teach embodiments wherein the VH region is amino-terminal to the VL region and wherein the VH region is carboxy-terminal to the VL region (See ¶0653). Regarding claims 63 and 72: Following the discussion of claims 1, 3, 26-27, 49, 54, and 64, Mujacic et al. teach that a therapeutically effective amount of cells expressing the CAR can be formulated with a pharmaceutically acceptable excipient for administration to a subject (See ¶0055, 0102, 0463, 0469). The cells can be administered for treating a subject with a disease such as cancer (See ¶0538-0539, 0778, and 0788). Claims 1, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, 72, and 75 remain rejected under 35 U.S.C. 103 as being unpatentable over Mujacic et al. (WO 2019113557 A1), of record, in view of Balderes et al. (US 7951370 B2), of record, further in view of Forman et al. (US 20160333108 A1), of record. The teachings of Mujacic et al. and Balderes et al. are set forth in the rejection above and are incorporated herein in their entirety. Regarding claim 75: Following the discussion of claims 1, 3-5, 11-12, 14, 18-19, 23-24, 26-27, 49, 54, 63-64, and 72, Mujacic et al., modified by Balderes et al., render obvious an anti-tyrosinase CAR but do not expressly teach the CAR as comprising a spacer having the sequence of instant SEQ ID NO 16. Forman et al. teach a CAR spacer derived from a modified IgG4 Fc region triple mutated to comprise S228P, L235E and N297Q mutations (See ¶0050-0052, SEQ ID NO 19, and alignment below (first 120 aa displayed)) which is identical to the sequence of instant SEQ ID NO 16. PNG media_image3.png 212 716 media_image3.png Greyscale It would have been obvious to one having ordinary skill in the art prior to the effective filing date of the claimed invention to modify the CAR of Mujacic et al., modified by Balderes et al., to substitute the spacer taught by Forman et al. Substitution of one known element for another known element is considered to be prima facie obvious, absent a showing that the result of the substitution yields more than predictable results. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to JENNIFER S SPENCE, whose telephone number is 571-272-8590. The examiner can normally be reached M-F 8:30-5:30. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Christopher M Babic, can be reached at 571-272-8507. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /J.S.S./Examiner, Art Unit 1633 /CHRISTOPHER M BABIC/Supervisory Patent Examiner, Art Unit 1633
Read full office action

Prosecution Timeline

Mar 03, 2022
Application Filed
Mar 03, 2022
Response after Non-Final Action
Sep 19, 2022
Response after Non-Final Action
Feb 06, 2025
Non-Final Rejection — §103
May 14, 2025
Response Filed
Aug 06, 2025
Final Rejection — §103
Nov 12, 2025
Response after Non-Final Action
Dec 12, 2025
Request for Continued Examination
Dec 15, 2025
Response after Non-Final Action
Mar 06, 2026
Non-Final Rejection — §103
Mar 31, 2026
Interview Requested
Apr 14, 2026
Applicant Interview (Telephonic)
Apr 14, 2026
Examiner Interview Summary

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12600971
MODIFIED IMMUNE CELLS HAVING ADENOSINE DEAMINASE BASE EDITORS FOR MODIFYING A NUCLEOBASE IN A TARGET SEQUENCE
2y 5m to grant Granted Apr 14, 2026
Patent 12594302
Single Domain Antibodies and Their Use in Cancer Therapies
2y 5m to grant Granted Apr 07, 2026
Patent 12577283
KNOCKDOWN OR KNOCKOUT OF ONE OR MORE OF TAP2, NLRC5, B2m, TRAC, RFX5, RFXAP and RFXANK TO MITIGATE T CELL RECOGNITION OF ALLOGENEIC CELL PRODUCTS
2y 5m to grant Granted Mar 17, 2026
Patent 12551560
COMPOSITIONS AND METHODS FOR USE IN IMMUNOTHERAPY
2y 5m to grant Granted Feb 17, 2026
Patent 12534509
ENGINEERED IMMUNE CELLS WITH RECEPTOR CROSS-TALK
2y 5m to grant Granted Jan 27, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

AI Strategy Recommendation

Get an AI-powered prosecution strategy using examiner precedents, rejection analysis, and claim mapping.
Powered by AI — typically takes 5-10 seconds

Prosecution Projections

3-4
Expected OA Rounds
67%
Grant Probability
99%
With Interview (+45.1%)
3y 10m
Median Time to Grant
High
PTA Risk
Based on 106 resolved cases by this examiner. Grant probability derived from career allow rate.

Sign in with your work email

Enter your email to receive a magic link. No password needed.

Personal email addresses (Gmail, Yahoo, etc.) are not accepted.

Free tier: 3 strategy analyses per month