Prosecution Insights
Last updated: April 19, 2026
Application No. 18/381,081

NON-HLA RESTRICTED T CELL VACCINE FOR TCR GAMMA ALTERNATE READING FRAME PROTEIN (TARP) PROTEIN EXPRESSING CANCERS

Non-Final OA §102§103§112
Filed
Oct 17, 2023
Examiner
BUCCINI, MICHELLE CALLAHAN
Art Unit
1675
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Pds Biotechnology Corporation
OA Round
1 (Non-Final)
Grant Probability
Favorable
1-2
OA Rounds
3y 2m
To Grant

Examiner Intelligence

Grants only 0% of cases
0%
Career Allow Rate
0 granted / 0 resolved
-60.0% vs TC avg
Minimal +0% lift
Without
With
+0.0%
Interview Lift
resolved cases with interview
Typical timeline
3y 2m
Avg Prosecution
7 currently pending
Career history
7
Total Applications
across all art units

Statute-Specific Performance

§101
11.5%
-28.5% vs TC avg
§103
26.9%
-13.1% vs TC avg
§102
19.2%
-20.8% vs TC avg
§112
30.8%
-9.2% vs TC avg
Black line = Tech Center average estimate • Based on career data from 0 resolved cases

Office Action

§102 §103 §112
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. Information Disclosure Statement The information disclosure statement submitted on 12/06/2023, 9/23/25 and 06/26/2024 fails to comply with 37 CFR 1.98(a)(2), which requires a legible copy of each cited foreign patent document; each non-patent literature publication or that portion which caused it to be listed; and all other information or that portion which caused it to be listed. T he information lined through therein has not been considered. In IDS 12/06/2023, the Sayour NPL document is too grainy to read. Claim Objections Claims 23, 24, 29, 30, 35, 37, 38, 39, and 63 are objected to because of a typo of the word immunogenic. Claims 39 and 63 are objected to because peptide should be singular in: “at least one peptides”. Claim 63 is objected to because it has a period in the middle of the claim and because it repeats “at least one multiepitope peptide” . 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. Claim 20 is rejected as indefinite because the phrase “mixed as separate micelles” is unclear. Examiner is interpreting this to mean that micelles, containing one or more multiepitope peptides, are mixed with cationic lipid nanoparticles. Claim 21 is rejected as indefinite because the phrase “mixed at a 1:1 ratio” is unclear. For the purposes of examination and based on the specification, E xaminer will be interpreting this as a 1:1 ratio by volume. Furthermore, Examiner is interpreting that the multiepitope peptides in Claim 21 are contained within micelles, since it is dependent from Claim 20. Claim 24 is rejected as indefinite for lack of antecedent basis. It refers to “the at least one multiepitope peptide” of Claim 23, but Claim 23 only recites “a multiepitope peptide”. For the purpose of examination, this claim will be interpreted to be: “The immunogenic composition of claim 23, wherein the multiepitope peptide comprises an amino acid sequence with at least 80% sequence identity with any one of SEQ ID NOs: 27-30, and 32.” Claim 63 is rejected as indefinite because it claims the “composition of claim 23”; however , explicit recitation of the composition does not match that of Claim 23 . Claim 23 recites, “a multiepitope peptide comprising at least one… TARP peptide…” while C laim 63 recites, “at least one multiepitope peptide comprising at least one TARP peptide.” The language of claim 23 is drawn to a single multiepitope peptide while the language of claim 63 includes an embodiment of multiple different multiepitope peptides. For the purposes of claim interpretation, C laim 63 will be interpreted as having consistent language with claim 23: “ a multiepitope peptide comprising at least one TARP peptide…” 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. Claims 1 , 7 , 10, 24 , 39 and 63 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. Claims 1, 7, 10, and 24 are drawn to a multiepitope peptide comprising an amino acid sequence with at least 80% sequence identity with any one of SEQ ID NOs: 27-30 and 32. In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant has possession of and what Applicant is claiming. In order to provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. In the instant case, a multiepitope peptide with at least 80% identity to different amino acid sequences results in a genus of possible peptides. From the specification, amino acid sequence alterations can include insertions, deletions, or substitutions of the protein backbone [0067]. SEQ ID NO: 28 is 32 amino acids long. Any combination of these amino acid residues could be inserted, deleted, or substituted with any of the other 19 possible amino acid residues so long as the variant comprises 80 % sequence identity to SEQ ID NO: 28 . Further conservative substitutions are tolerable as well. The benefit of the present invention is that the inclusion of various epitopes makes it effective despite variation in human leukocyte antigen allele expression across individuals [0008]; however, the claim language is drawn such that the majority of an epitope, such as SEQ ID NO: 2, could be altered or deleted, counteracting the benefit of a multiepitope composition. Furthermore, the breadth of the claim language means that there are millions of possible combinations that would result in 80% sequence identity for SEQ ID NO: 28 alone. The specification does not provide examples or adequate description of other species besides that of SEQ ID NOs: 27-30 and 32. In other words, the Applicant has not demonstrated any examples in which sequence alteration of the disclosed sequences would result in the same immunogenic response. 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. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (MPEP § 2163.05). In the absence of sufficient recitation of distinguishing identifying characteristics or structure-to-function attributes for the entire genus, the specification does not provide adequate written description of the claimed genus. Therefore, in view of the case law directed to an appropriate number of representative species, claims 1 , 7, 10 and 24 are rejected for insufficient written description. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. § 112 is severable from its enablement provision (see page 1115). Claim 39 is directed towards “treating cancer.” First, Applicant does not have possession of treating every cancer. Applicant has not demonstrated possession of treating a single cancer model and therefore cannot possibly have possession of the entire cancer genus, which includes a variety of mechanistically different and organ/system-specific conditions. Furthermore, the multiepitope peptide is specifically designed for cancers overexpressing T-cell receptor gamma alternate reading frame protein ( TAR P ) ; however, TARP overexpressing cancers do not constitute the genus of all cancers . Therefore, the specification does not satisfy the written description requirement for treating every cancer. Furthermore, the specification does not satisfy the written description requirement for treating cancer. According to the specification, “treating ” includes curing and lessening symptoms of a pathologic condition, as well as taking preventative measures for a condition [0111]. There is no disclosure of curing or prevent ing cancer in the specification. In addition , the specification does not demonstrate possession of lessening the symptoms (ex. diminished tumor growth) of a pathologic condition. While the specification has demonstrated that administration of a multiepitope peptide is sufficient to induce an immunogenic response, the specification is not sufficient to demonstrate that administration of the multiepitope peptide resulted in clinical benefit. Therefore, specification does not demonstrate possession of treating cancer. Claim 63 is directed toward a “polyfunctional cytolytic T cell response.” Minton, Nature Reviews Immunology, Mechanisms of T cell polyfunctionality, 201 3 , defines polyfunctional T cells as “ having the ability to secrete cytokines and chemokines and to mediate cytolysis ” (abstract). While the instant disclosure certainly demonstrates that the long TARP peptides elicit an immune response through production of the cytokine IFN-gamma, A pplicant has not shown that this is specifically a polyfunctional cytolytic T cell response. First, the production of IFN-gamma as shown is not specifically attributable to T cells in the sense that natural killer cells producing IFN-gamma would also contribute to this result. In other words, the IFN-gamma production is not measured solely from T cells but rather any cell that produced IFN-gamma in response to the stimulus. Moreover, there is no evidence in the disclosure to suggest that the composition of Claim 23 results in a cytolytic response , where cancerous cells are killed. For example, there is no disclosure demonstrating decreased tumor volume, a degranulation assay, or chromium release assays, which would demonstrate not just an activated immune response, but indicate tumor cell death . Claims 1 , 7, 10, 24 , 39, 54-57, 59-61 , and 63 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 enablement requirement. While the specification is enabling for a multiepitope peptide with at least 95% sequence identity to any of SEQ ID NOs: 27-30 and 32, it is not enabling for a multiepitope peptide with at least 80% of the claimed sequences. Furthermore, the specification is not enabling for treating cancer or inducing a polyfunctional cytolytic T cell response by administering the claimed multiepitope peptide composition. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention. MPEP § 2164.01(a) states that there are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue”. These factors include, but are not limited to: A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. In re Wands, 8 USPQ2d, 1400 (CAFC 1988) and MPEP 2164.01. Claims 1, 7, 10 and 24 encompass a multiepitope peptide with the at least 80% sequence identity to any of SEQ ID NOs: 27-30 and 32. The breadth of the claims According to the specification, a ny combination of these amino acid residues could be inserted, deleted, or substituted with any of the other 19 possible amino acid s so long as the variant comprises 80 % sequence identity to the claimed sequences. Further conservative substitutions are tolerable as well [0067]. Therefore, the claimed invention is extremely broad because the scope of the claim represents millions of embodiments. The nature of the invention The nature of the claimed invention is peptide s comprising multiple epitopes (i.e. binding regions ) of the TARP protein . In some embodiments , peptides have overlapping regions and are administered together . For example, SEQ ID NOs: 27 and 28 both contain the epitope represented by SEQ ID NO: 2. The amount of direction provided by the inventor and the state of the prior art Applicant does not teach , for example, how up to 7 residues can be mutated in SEQ ID NO: 28 to result in multiepitope peptide capable of producing an immunogenic response . The number of mutations generally possible in any given protein that can be made with a reasonable expectation of success are limited. Certain positions in the sequence are critical to the protein's structure/function relationship, e.g., such as various sites or regions directly involved in binding, activity and in providing the correct three-dimensional spatial orientation of binding and active sites. The art provides evidence that mutations can be destabilizing and their effects unpredictable. Bhattacharya et al. (PLoS ONE 12(3): e0171355. https://doi.org/10.1371/journal.pone.0171355 ; 22 pages total) teach even single nucleotide variations have a “range of effects at the protein level that are significantly greater than assumed by existing software prediction methods, and that correct prediction of consequences remains a significant challenge” (p. 18, 1 st and 2 nd paragraphs). In addition, Fenton et al. (Medicinal Chemistry Research (2020) 29:1133–1146) review the unpredictability of making substitutions at non-conserved positions in a protein, which can have significant effects on protein function, that computational algorithms cannot predict very well (p. 1134, right column, middle paragraph). Although machine learning algorithms have improved the ability to predict protein 3D structure from sequences, methods based on artificial intelligence for predicting the impact of mutations on protein stability still face challenges, including prediction biases towards “generalization”, “data set”, “destabilizing mutations” and the inability to predict the effects of multiple mutations. See Figure 1, at p. 162 and the discussion at pages 165-166 of Pucci et al. (Current Opinion in Structural Biology 2022, 72: 161-168). Even in the case of single mutations, artificial intelligence programs do not accurately “predict the impact of mutation on protein stability” or function (see p. 2, 2 nd paragraph and p. 7, 1 st full paragraph of Pak et al., PLoS ONE 18(3): e0282689. https://doi.org/10.1371/journal.pone.0282689 ). In the instant case, the claims encompass up to a 20 % divergence from SEQ ID NO s : 27-30 and 32 , which in practical terms constitutes deletion or substitution of up to 9 amino acid residues. Applicant ha s provided little or no guidance to enable one of ordinary skill in the art to determine, without undue experimentation, the positions in the protein which are tolerant to change by amino acid substitutions or deletions, and the nature and extent of changes that can be made in these positions. There is not adequate guidance as to the nature of active derivatives that may be constructed beyond merely an invitation to the artisan to use the current invention as a starting point for further experimentation. Conclusion Altogether, Claims 1, 7, 10, and 24 are not enabled for a multiepitope composition that contains 80% sequence identity to SEQ ID NOs: 27-30 and 32 . Given the degree to which amino acid change s can have unanticipated effects on the function of a peptide, particularly if it occurs in the epitope binding region, one of ordinary skill in the art would not have a reasonable expectation of success making and using the claimed invention. However, b ecause the nature of the invention includes some overlap (i.e. two multiepitope peptides contain the same epitope sequence) one of ordinary skill in the art would have a reasonable expectation of success by a very limited amount of variation. Therefore, Claims 1, 7, 10, and 24 are enabled for a multiepitope composition that contains 95% sequence identity to SEQ ID NOs: 27-30 and 32. Claim 39 and 54-57, 59-61, and 63 are drawn towards a method of treating cancer or inducing a polyfunctional cytolytic T cell response in a subject by administering the immunogenic composition of C laim 23 , namely a multiepitope peptide . According to the specification ([0032]), one embodiment of “treating cancer” , as recited in Claim 39 , includes inducing a TARP-specific polyfunctional cytolytic T Cell response, as recited in Claim 63. Therefore, the enablement analysis for these claims will be combined because a lack of enablement for inducing a cytolytic response is also, in at least one embodiment, a lac k of enablement for treating cancer . The breadth of the claims and nature of the invention: The broadest reasonable interpretation of Claim 39 includes a method of curing any cancer with the immunogenic composition of Claim 23. The specification defines treatment not only as therapeutic measures that alleviate symptoms of a pathologic condition, but also as curing a condition and preventative measures for individuals who may ultimately acquire the disorder [0111]. Furthermore, the specification does not limit what cancer the therapeutic measure is implemented to treat or what the subject is . The broadest reasonable interpretation of Claim 63 is that administration of the immunogenic composition of Claim 23 in a subject induce s a polyfunctional cytolytic T cell response. Therefore, the claimed invention is broad. One of ordinary skill in the art would recognize that there is not one composition that could not cure every type of cancer. Furthermore, Applicant admits in the specification that TARP is an ideal target antigen for therapeutic vaccination because it is overexpressed in cancers like prostate and breast cancers, but with little expression in normal cells [0005]. It would follow then that cancers not expressing TARP would not respond to TARP targeting. The state of the art only points to TARP overexpression in prostate cancer, breast cancer, endometrial cancer, salivary gland tumors and acute myeloid leukemia (AML) ( Vanhooren, pg. 3062, left side, middle of paragraph). When analyzing the scope of enablement, the claims are analyzed with respect to the teachings of the specification and are to be "given their broadest reasonable interpretation consistent with the specification." See MPEP 2111 [R-5]; Phillips v. AWH Corp., 415 F.3d 1303, 75 USPQ2d 1321 (Fed. Cir. 2005); and In re Hyatt, 211 F.3d 1367, 1372, 54 USPQ2d 1664, 1667 (Fed. Cir. 2000). Applicant always has the opportunity to amend the claims during prosecution, and broad interpretation by the examiner reduces the possibility that the claim, once issued, will be interpreted more broadly than is justified. In re Prater, 415 F.2d 1393, 1404-05, 162 USPQ 541, 550- 51 (CCPA 1969). The state of the prior art and level of predictability in the art: While Applicant has demonstrated that the composition containing SEQ ID NO: 2 7 and 28 was sufficient to induce an immunogenic response (Fig. 1) , Applicant has not demonstrated that this has translated into induction of a cytolytic T cell response ; the state of the art at the time of filing was not sufficient to resolve the lack of disclosure and enable one of ordinary skill in the art to effectively treat a subject . T he prior art recognized INF-gamma release as indicative of an imm un ogenic response, but this is distinct from a cytolytic T cell response that results in clinical benefit . For example, Rittig et al., demonstrated immunological response to a tumor-associated antigen (TAA) targeting mRNA vaccine using INF-gamma measurement (Figure 3), but demonstrated cytotoxic activity from activated T cells using chromium-release assays (Figure 4) . Leading up to the filing date, one of ordinary skill in the art would have been taught away by Berzofsky et al., 2013 from using T cell activation (ie. INF-gamma production) as a correlation with patient outcome , as measured by prostate-specific antigen (PSA) velocity : “ About 77% of study subjects developed TARP-specific CD8 + T cell responses, but these responses did not correlate with decreased slope and slowing in PSA velocity ” (pg. 1117, left side, 9 lines up from bottom paragraph). In fact, it wasn’t until a few weeks after the instant effective filing date that those same authors were able to elucidate a correspondence between high IFN-gamma and clinical benefit: “ The ability of high IFN-gamma ELISPOT response to the vaccine peptides to predict clinical responsiveness as measured by decreased PSA-slope log supports a protective role of antigen-specific T cells ” (Olkhanud et al., Results and Conclusion). Altogether, the specification has not taught a cytolytic T cell response, or treating cancer through another mechanism. Based on the teachings of the prior art at the time of filing, one of ordinary skill in the art would not have a reasonable expectation of success based simply on the evidence in the specification that the multiepitope composition was immunogenic. Level of skill in the art: The level of skill would be high encompassing vaccine development , immunotherapy, etc. Amount of direction provided by inventor and the existence of working examples: The specification and working examples demonstrate that specific combinations of long peptides can result in an immunogenic response in vivo. However, the immunogenic response was only tested in healthy mice, not in a disease model. Furthermore, none of the examples are directed toward treating a subject. For example, tumor regression was not assessed and cytotoxic activity is not specifically measured. There is no guidance with respect to the dosage , administration schedule, etc. The quantity of experimentation needed to make or use the invention based on the content of the disclosure: In light of the unpredictability surrounding the claimed subject matter, the undue breadth of the claimed invention’s intended use, and the lack of adequate guidance, one wishing to make and practice the presently claimed invention would be unable to do so without engaging in undue experimentation. Conclusion Altogether, Claims 39 and 54-57, and 59-61 are not enabl ed for treating cancer by administering the claimed composition, nor as a therapeutic option for every cancer. Furthermore, Claim 63 is not enabled for inducing a polyfunctional cytolytic T cell response in a subject . Undue experimentation would be required to demonstrate that the claimed composition is able to induce a cytolytic response or otherwise treat a cancerous condition, let alone cure or prevent it. Claim 61 is drawn to a method of treating cancer further comprising administering anti-cancer targeted therapy comprising a histone deacetylase (HDAC) inhibitor. The breadth of the claims and nature of the invention: While the breadth of the claim is reasonable, the nature of the invention at the time of filing was not understood well enough for one of ordinary skill in the art to be able to successfully use the claimed invention based on the current disclosure. The state of the prior art and level of predictability in the art: At the time of filing, the implementation of HDAC inhibitors with additional anti-cancer therapies had mixed results. A review by Sur a weera et al., 2018, summarizing the research of HDAC inhibitor combination therapy did not address multiepitope peptide vaccines or even cancer vaccines more broadly as implemented in combination with HDAC inhibitors, suggesting that the implementation and subsequent effects of pairing the two anti-cancer treatments was not routine or well known in the art. Bad a mchi-Zadeh et al., did demonstrate that a combination of HDACs and bromodomain and extraterminal proteins (BET) significantly increases vaccine-elicited CD8+ T cell numbers on protein based vaccines for melanoma. Bad a mchi-Zadeh et al., specifically states that this study was the first to asses viral vectored and protein-based vaccines, rather than cell - based cancer vaccines . Rana et al, 2020 teaches that HDAC inhibitors failed to treat solid tumors like prostate cancer (abstract). One of the examples of an HDAC inhibitor from the instant specification (pg. 32) is Romidepsin, which Rana specifically teaches failed to continue to a phase III trial for prostate cancer “due to a majority of patients exhibiting either toxicity or disease progression” (abstract). Altogether, these results teach an underdeveloped field for HDAC inhibitors at the time of filing where one of ordinary skill in the art would not have a reasonable expectation of success in its implementation as a therapeutic , particularly for the treatment of prostate cancer, and more particularly if used in combination with multiepitope peptide compositions , which had not been the focus of HDAC inhibitor research leading up to that point . Level of skill in the art: The level of skill would be high encompassing vaccine development, immunology , immunotherapy, etc. Amount of direction provided by inventor and the existence of working examples: None of the working examples or figures in the instant specification are drawn to the successful implementation of HDAC inhibition as a combination treatment with the instant multiepitope peptide compositions. The language in the specification of HDAC inhibitors is purely descriptive, and posited more as a suggestion than an explanation to one of ordinary skill in the art on how to successfully implement the claimed embodiment. For example, Kroesen et al. provides motivation to one of ordinary skill in the art to pursue HDAC inhibitor treatment with immunotherapy, but also cites several important considerations, which have not been addressed in the instant specification, to ensure its success , such as the timing of HD A C inhibitor administration and the class of HDAC inhibitors chosen (Figure 1). The quantity of experimentation needed to make or use the invention based on the content of the disclosure: In light of the unpredictability surrounding the claimed subject matter, and the lack of adequate guidance, one wishing to make and practice the presently claimed invention would be unable to do so without engaging in undue experimentation. Conclusion Altogether, Claim 61 is not enabled for treating cancer with a multiepitope peptide in combination with an HDAC inhibitor because given the state of the art and the detail within the disclosure, one of ordinary skill in the art would not have a reasonable expectation of success without undue experimentation. Cl aim Rejections - 35 USC § 102 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 the appropriate paragraphs of pre-AIA 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. Claim(s) 1 and 7 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Wood et al, US10286050 (hereafter Wood ‘050). Claim 1 recites a multiepitope peptide comprising at least one multiepitope peptide fragment with an amino acid sequence with at least 80% sequence identity of any one of SEQ ID NOs: 27-30 and 32. Claim 7 is drawn to multiepitope peptide modifications including palmitoylation. As discussed previously, the specification is only enabling for sequences comprising at least 95% identity to the claimed SEQ ID NOs: 27-30 and 32. The definition of a multiepitope peptide according the instant specification is a “peptide or polypeptide that includes at least two epitopes as described herein” [0068]. SEQ ID NOs: 27-30 and 32 are themselves multiepitope peptides, because they contain multiple TARP epitopes (SEQ ID NOs: 2-8). Therefore, a reference that teaches at least 95 % of any of SEQ ID NOs: 27-30 and 32 would read on Claim 1. Wood ‘050 teaches SEQ ID NO: 1, which teaches 98.4% identity of instant SEQ ID NO: 27 (see below). Wood also teaches that modification of a peptide including palmitoylation: “Lipids have been identified as agents capable of assisting in priming CTLs in vivo against various antigens…palmitic acid residues can be … linked… to an immunogenic peptide. The lipidated peptide can then be injected directly in a micellar form, incorporated in a liposome, or emulsified in an adjuvant” (Column 20 lines 24-33). Therefore, Claims 1 and 7 are anticipated by Wood ‘050. 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. Claims 9, 10, 16, 17, 19 , 23, 24, 29, 30 , and 35 is/are rejected under 35 U.S.C. 103 as being unpatentable over Wood ‘050 in view of Bedu-Addo et al., US 20190358318 (hereafter Bedu-Addo ‘ 318 ) . Claims 9, 10, 23, and 24 recite a composition of one or more multiepitope peptides, comprising at least one TARP peptide comprising an amino acid sequence with at least 80% sequence identity of any one of SEQ ID NOs: 27-30 and 32. As discussed previously, the specification is only enabling for sequences comprising at least 95% identity to the claimed SEQ ID NOs: 27-30 and 32. Claims 23 and 24 further limit that the composition is immunogenic. Claims 16 and 29 further limit that the TARP peptides have an amino acid sequence comprising any of SEQ ID NOs: 2-8. Claims 17 and 35 further comprise a cationic lipid adjuvant, wherein the cationic lipid includes DOTAP. Claim s 19 and 30 further limit that the multiepitope peptide is modified by palmitoylation. Wood ‘050 teaches SEQ ID NO: 1, which teaches 98.4% identity of instant SEQ ID NO: 27, as applied above. Wood ‘050 also teaches palmitoylation modification of peptides, as applied above. Wood ‘050 further teaches that the multiepitope peptide comprises TARP peptides with 100% identity to instant SEQ ID NO: 2, 4-8 (see below). INSTANT SEQ ID NO: 2 INSTANT SEQ ID NO: 4 INSTANT SEQ ID NO: 5 INSTANT SEQ ID NO: 6 INSTANT SEQ ID NO: 7 INSTANT SEQ ID NO: 8 While Wood ‘050 teaches an adjuvant in TARP peptide compositions , it does not teach specifically a cationic lipid adjuvant, wherein the lipid includes DOTAP. Bedu-Addo ‘318 teaches a vaccine comprising a cationic lipid adjuvant, wherein embodiments of the cationic lipid include DOTAP, DOEPC, DOTMA, R-DOTAP, R-DOEPC, R-DOTMA, S-DOTAP, S-DOEPC, and S-DOTMA and an antigen, wherein the antigen is a cancer antigen (pg. 10, [0355]). It further teaches contemplation of structural variants and derivatives of the disclosed cationic lipids (pg. 11, first paragraph). It further teaches that cationic lipid adjuvants can elicit a n enhanced T cell response: “cationic lipids act as potent immunomodulatory adjuvants and induce superior CD8+ T-cell immune responses compared to the emulsion adjuvant Montanide™” (pg. 16, [0422]). Wood teaches a multiepitope peptide and an adjuvant to enhance antigen presentation. Bedu-Addo discloses a benefit of a cationic lipid adjuvant over a traditional adjuvant formula in the field of endeavor, namely vaccine development. One of ordinary skill in the art would have been motivated to combine the teachings of a cationic lipid described in Bedu-Addo ‘318 , with the multiepitope peptide described by Wood ‘050 in order to enhance the immunogenicity of the composition taught by Wood ‘050 . Claims 20, 21, 37 and 38 is/are rejected under 35 U.S.C. 103 as being unpatentable over Wood ‘050 in view Bedu-Addo ‘318 , as applied above, in further view of Gandhapudi et al., The Journal of Immunology, 2019 (hereafter Gandhapudi). Claims 20, 21, 37 , and 38 recite the multiepitope peptides mixed as separate micelles with preformed cationic lipid nanoparticles at a 1:1 ratio by volume. Wood ‘050 and Bedu-Addo ‘318 teach all the limitations of Claim 9 and 23, as applied above, from which Claim s 20, 21, 37 and 38 depend . Specifically, Wood ‘050 teaches that peptides can be injected into a micelle (Column 20, lines 20 -35) to aid in inducing a cellular response. Furthermore, Bedu-Addo ‘318 teaches that a cationic lipid adjuvant can elicit a n enhanced T cell response compared to a traditional adjuvant formula (pg. 16, [0422]). However, Wood ‘050 and Bedu-Addo ‘318 do not teach that the micelles and cationic lipid nanoparticles are mix ed at a 1:1 ratio by volume. Gandhapudi teaches mixing equal volume of R-DOTAP nanoparticles with peptides of interest (pg. 3525, right side, last paragraph). Gandhapudi teaches a known method of mixing peptides with cationic lipid nanoparticles. One of ordinary skill in the art would have been motivated to substitute the peptides of Gandhapudi , with micelles containing peptides , based on motivation in Wood ‘050 that the micellular form enhances cellular response. All of the sources are in the same field of endeavor, namely vaccine development. Claims 9 and 22 is/are rejected under 35 U.S.C. 103 as being unpatentable over Wood ‘050 and Bedu-Addo ‘318, as applied above, in further view of Berzovsky et al., US 7541035 (hereafter Berzovsky ‘ 035 ). Claim 22 is drawn to a multiepitope peptide composition comprising an enhancer agonist epitope. Examiner is interpreting the phrase “enhancer agonist epitope” to mean an epitope that has been modified to improve its efficacy within a composition by, for example, increasing affinity of the peptide for MHC molecules or increasing T cell receptor triggering. Wood ‘050 and Bedu-Addo ‘318 teach all the limitations of Claim 9, as applied above, from which Claim 22 depends. Wood ‘050 and Bedu-Addo ‘318 do not teach an enhancer agonist epitope. Berzovsky ‘ 035 teaches immunogenic TARP polypeptides for treating prostate and breast cancer. Specifically, it teaches that SEQ ID NO: 6, equivalent to instant SEQ ID NO: 3 (see below), is an enhanced peptide in compared to wild type version of the sequence in terms of binding affinity (Fig. 3c) and immunogenicity ( F ig . 4A). Furthermore, Berzovsky ‘ 035 specifically teaches why this sequence is preferable over the other enhanced peptides: “When compared quantitatively (FIGS. 4C and 4D), TARP-29-37-9V (SEQ ID NO: 6) was the most immunogenic of the peptides in inducing CTLs specific for the wild-type sequence. Thus, TARP-29-37-9V (SEQ ID NO: 6) could be the most potent of the immunogens for inducing CTLs against tumor cells expressing the natural antigen” (Column 37, lines 1-9). Instant SEQ ID NO: 3 Berzovsky ‘035 teaches that epitope enhancement was known in the art as a technique to improve the immunogenicity of peptide epitopes. Based on the benefits described in ‘035 of instant SEQ ID NO: 3, one of ordinary skill in the art would have been motivated to incorporate it into a multiepitope peptide composition to maximize efficacy. Conclusion No claims allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT MICHELLE C BUCCINI whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-1352 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 7:30-5 EST . 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, FILLIN "SPE Name?" \* MERGEFORMAT Jeffrey Stucker can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 5712720911 . 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. /MICHELLE CALLAHAN BUCCINI/ Examiner, Art Unit 1675 /JEFFREY STUCKER/ Supervisory Patent Examiner, Art Unit 1675
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Prosecution Timeline

Oct 17, 2023
Application Filed
Nov 06, 2025
Response after Non-Final Action
Mar 31, 2026
Non-Final Rejection — §102, §103, §112 (current)

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Prosecution Projections

1-2
Expected OA Rounds
Grant Probability
3y 2m
Median Time to Grant
Low
PTA Risk
Based on 0 resolved cases by this examiner. Grant probability derived from career allow rate.

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