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. Election/Restrictions Applicant’s election without traverse of invention I and the required species in the reply filed on 8/14/25 is acknowledged. The elected species are the TMP of claim 106 a1 and b1 and the MOD is a cytokine. Claim s 111-124 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions , there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 8/14/25 . Claims 105-110 are examined on the merits. Information Disclosure Statement The information disclosure statement (IDS) submitted on 10/18/22, 12/14/22, 1/24/23, 4/27/23, 7/27/23, 8/25/23, 8/29/23, 9/28/23, 10/5/23, 11/7/23, 12/12/23, 1/12/24, 1/30/24, 2/16/24, 4/17/24, 9/10/24, 10/14/24, 10/16/24, 11/7/24, 12/18/24, 2/28/25, 4/3/25, 6/16/25, 8/14/25 and 9/25/25 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Specification The specification is objected to as failing to provide proper antecedent basis for the claimed subject matter. See 37 CFR 1.75(d)(1) and MPEP § 608.01(o). Correction of the following is required: claim 110 recites, “A homodimer comprising a first and a second heterodimer…”. However the specification does not mention a homodimer comprising a first and a second heterodimer. Claim Objections Claims 106 , 108 and 109 are objected to because of the following informalities: these claims begin with “A TMP of claim 106…”, however, since they depend from claim 106, these claims should recite, “The TMP of claim 106…” . Appropriate correction is required. 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 appl icant regards as his invention. Claims 105-110 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 105 requires a SARS-CoV-2 peptide, which is about 4 to about 25 amino acids in length. However, claims and specification do not define what the metes and bounds of “about” with regard to amino acid length of a peptide. Therefore, it is unclear what length of peptide is excluded by this limitation. Claims 107 recites, “a Cys residue at position 84 in the MHC class I heavy chain polypeptide”; “a Cys residue at position 12 in the B2M polypeptide”; “a Cys residue at position 236 in the MHC Class I heavy chain polypeptide” and claim 109 recites, “other than a histidine at position 16” and “other than a phenylalanine at position 42”. However, since each polypeptide does not possess a strict length or unique amino acid sequence, it is unclear if these amino acid positions are relative to a full-length polypeptide, a fragment thereof or if the amino acids are relative to the amino or carboxy terminus. Therefore, it is suggested that the claims be amended to include a corresponding SEQ ID NO: for each polypeptide. Claim 110 recites, “A homodimer comprising a first and second heterodimer…” However, if a first heterodimer and a second heterodimer were bound to each other, it is unclear how these proteins could also be a homodimer. The homodimer would involve two proteins that are identical, while the first and second heterodimers possess two distinct proteins each. Therefore, combining the first and second heterodimers would yield a hetero quadrimer. In addition, the specification does not elaborate on what a homodimer is. Claim 110 recites, “wherein the first and second heterodimers are covalently bound by one or more disulfide bonds between the Ig Fc polypeptides of the first and second heterodimers.” However, the dimer of claim 105 only possesses an Ig Fc on the second heterodimer, and therefore it is unclear how one or more disulfide bonds between two Ig Fc polypeptides when only one is present. 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. 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. Claim s 105, 106 and 108 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Seidel et al. (US PGPub 2017 / 0058015), in view of Li et al. (bioRxiv, 2020) . The claimed invention is drawn to a T cell modulatory polypeptide (TMP) comprising: at least one heterodimer: a first polypeptide comprising: a SARS-CoV-2 peptide, which is about 4 to about 25 amino acids in length; a Beta 2 microglobulin (B2M) polypeptide; a cysteine (Cys)-containing linker that links the SARS-CoV-2 peptide to the B2M polypeptide; a second polypeptide comprising: an MHC class I heavy chain polypeptide; one or more cytokines; and an immunoglobulin Fc polypeptide; wherein the first polypeptide and the second polypeptide are covalently linked to one another via at least a first and second disulfide bond, wherein the first disulfide bond is formed between (i) the Cys residue in the Cys-containing linker between the SARS-CoV-2 peptide and the ß2M polypeptide, and (ii) a Cys residue in the MHC class I heavy chain polypeptide; and the second disulfide bond is formed between a Cys residue in the ß2M polypeptide and a Cys residue in the MHC class I heavy chain polypeptide. The first polypeptide is in the N- to C -terminus order of SARS-CoV-2 peptide : Cys containing linker: B2M polypeptide and the second polypeptide is in the N- to C- terminal order of Cytokine: MHC class I heavy chain polypeptide: an Ig Fc polypeptide. The Prior Art Seidel et al. teach the generation of heterodimeric protein complexes that comprise a polypeptide comprising a candidate epitope of an antigen of a pathogen linked to a B2M vi a a Cys linker and a polypeptide comprising a cytokine (MOD) linked to a MHC class I heavy chain, which is linked to an Ig Fc polypeptide. [see Figure 2C and paragraphs 16, 17, 21, 23, 34, 107, 117, 126 and 259] Examples of pathogens that the epitopes are from include viruses and bacteria, such as human T-lymphotrophic virus-1 epitope LLFGYPVYV . [see paragraphs 42 and 124] In addition, the candidate epitope comprises 7 to 20 amino acids or 8-17 amino acids in length. [see paragraphs 21, 113 and 122] Examples of MOD are cytokines, such as IL-2. [see paragraph 259] However, Seidel et al. do not teach that their epitope employed is from a SARS-CoV-2 peptide. Li et al. teach the identification of SARS-CoV-2 epitopes that bind to MHC class I, such as IPFAMQMAYR and FAMQMAYRF . [see page 9, 2 nd paragraph] It would have been obvious to one of ordinary skill in the art to modify the compositions taught by Seidel et al. in order to employ a SARS-CoV-2 peptide of 4 to 25 amino acids in length . One would have been motivated to do so, given the suggestion by Seidel et al. that candidate epitopes of 7 to 20 amino acids, such as epitopes of viral antigens, can be attached to B2M and these epitopes interact with MHC class I molecules (see figure 2A-2C) . There would have been a reasonable expectation of success, given the knowledge that SARS-CoV-2 epitopes of 9 or 10 amino acids were previously identified as T cell/MHC class I specific , as taught by Li et al. Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made. Claim (s) 105-109 are rejected under 35 U.S.C. 103 as being unpatentable over Seidel et al. (WO 201 9/051127 ) and Li et al. ( supra ) . The claimed invention is drawn to A T cell modulatory polypeptide (TMP) comprising: at least one heterodimer: a first polypeptide comprising: a SARS-CoV-2 peptide, which is about 4 to about 25 amino acids in length; a Beta 2 microglobulin (B2M) polypeptide; a cysteine (Cys)-containing linker that links the SARS-CoV-2 peptide to the B2M polypeptide; a second polypeptide comprising: an MHC class I heavy chain polypeptide; one or more cytokines; and an immunoglobulin Fc polypeptide; wherein the first polypeptide and the second polypeptide are covalently linked to one another via at least a first and second disulfide bond, wherein the first disulfide bond is formed between (i) the Cys residue in the Cys-containing linker between the SARS-CoV-2 peptide and the ß2M polypeptide, and (ii) a Cys residue at position 84 in the MHC class I heavy chain polypeptide; and the second disulfide bond is formed between a Cys residue at position 12 in the ß2M polypeptide and a Cys residue at position 236 in the MHC class I heavy chain polypeptide. The first polypeptide is in the N- to C -terminus order of SARS-CoV-2 peptide: Cys containing linker: B2M polypeptide and the second polypeptide is in the N- to C- terminal order of Cytokine: MHC class I heavy chain polypeptide: an Ig Fc polypeptide. The cytokine is a variant IL-2 with an amino acid other than histidine at position 16 and an amino acid other than phenylalanine at position 42. The Prior Art Seidel et al. also teach in figure s 6B and 6 F (see below) diagram s of their TMMP heterodimer s that comprises a first polypeptide comprising a n epitope linked to a B2M, and a second polypeptide comprising a MOD, linked to a MHC class I heavy chain, linked to a Fc region of an Ig. These two polypeptides are connected through a disulfide bond between the B2M and the MHC or between the Cys containing linker of epitope and B2M and the MHC class I heavy chain. Of note, in figure 6 CC-1 and CC-2 refer to chemical conjugation sites and the figure description for figure 6 states: “ The first polypeptide, the second polypeptide, or both the first and second polypeptides of the T-Cell-MMP may also comprise one or more chemical conjugation sites in addition to the site employed for the conjugation of the epitope ”. Seidel et al. specifically teach cysteine substitutions at positions 84, 139 and 236 of the MHC class I heavy chain. [see paragraph 186 ] Specific amino acids that are involved in a cysteine-cysteine disulfide bonds are amino acid residue 12 of B2M and amino acid residue 236 of MHC class I heavy chain [see paragraph s 131, 562] and amino acid 84 of the MHC class I heavy chain and the cysteine linker of the epitope and B2M (see figure 6-paragraph 12] Seidel teach that a MOD can be a cytokine, such as IL-2, with variants of IL-2 also disclosed, such as an IL-2 that does not possess a histidine at position 12 and does not possess a phenylalanine at position 42. [see paragraphs 173 and 429 ] Lastly, examples of epitopes of Seidel et al. teach as being useful in their TMMP composition are peptide epitopes about 4 amino acids to about 20 amino acids in length. [see paragraph 102] Viruses can also provide epitopes of interest, such as HPV E7 epitope or an epitope from hepatitis A or B . [see paragraph 230] However, Seidel et al. do not teach that their epitope employed is from a SARS-CoV-2 peptide. Li et al. teach the identification of SARS-CoV-2 epitopes that bind to MHC class I, such as IPFAMQMAYR and FAMQMAYRF . [see page 9, 2 nd paragraph] It would have been obvious to one of ordinary skill in the art to modify the compositions taught by Seidel et al. in order to employ a SARS-CoV-2 peptide of 4 to 25 amino acids in length. One would have been motivated to do so, given the suggestion by Seidel et al. that candidate epitopes of about 4 to about 20 amino acids, such as epitopes of viral antigens, can be attached to B2M and these epitopes interact with MHC class I molecules (see figure 6B and 6F ). There would have been a reasonable expectation of success, given the knowledge that SARS-CoV-2 epitopes of 9 or 10 amino acids were previously identified as T cell/MHC class I specific, as taught by Li et al. Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT BENJAMIN P BLUMEL whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-4960 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 8-5 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 Michael Allen can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT (571) 270-3497 . The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. 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