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 with traverse of Group I, claims 77-94, 97-98, and 100, drawn to a polypeptide antigen, and the species of SEQ ID NO: 3, in the reply filed on 1/23/2026 is acknowledged.
The traversal is on the ground(s) that the elected and non-elected groups are not “independent or distinct”, and examination of all claims together would not impose a serious search or examination burden. For example, independent claim 77 is directed to peptides comprising SEQ ID NO: 3, and the method-of-use claims in Group II each require the same peptide subject matter as a positive recitation. Thus, the method claims do not define a distinct invention, but simply recite a method of using the very same polypeptide that is the subject of Group I. Moreover, examination of the method claims would require searching the same peptide prior art needed to examine the product claims, since each method claim is limited to administering or otherwise using the peptide comprising SEQ ID NO: 3. Any additional search for method-of-use limitations would not rise to the level of a “serious” additional burden beyond that required to examine the product claims, particularly given the shared classification and common technical field. This is not found persuasive because, as indicated in the restriction requirement filed on 7/23/2025, the product can be used in a materially different process of using that product. Therefore, a serious search burden would be imposed on the Examiner if both inventions were examined.
The requirement is still deemed proper and is therefore made FINAL.
Claims 95-96 and 99 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 1/23/2026.
Applicant elected the species of SEQ ID NO: 3, which is free of the prior art of record. Accordingly, the Examiner is expanding the search to examine another claimed sequence, which is SEQ ID NO: 144.
Claims 77-94, 97-98, & 100 are under examination on the merits.
Information Disclosure Statement
The Information Disclosure Statement (IDS) submitted on 5/24/2023 is in compliance with 37 CFR 1.97. Accordingly, the IDS is being considered by the examiner.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code on p. 30, line 7. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Claim Objections
Claims 77, 79, and 80, are objected to because of the following informalities: claims 77, 79, and 80 recite multiple descriptions of the same peptide sequences (claim 77, line 2: “P3 peptide (SEQ ID NO: 3)”; claim 79, lines 2-3 “P3 (SEQ ID NO: 3), P3 L (SEQ ID NO: 43), SJ-FT (SEQ ID NO: 144) and P4/TMP-Pol3 (SEQ ID NO: 116)”). Instead, the claims should only recite the sequence identifiers associated with the sequence listing, for example, SEQ ID NO: 3 instead of “P3 peptide”, etc. 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.
Claim 97 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim 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.
Applicant in claim 97 broadly claims a nucleic acid encoding a polypeptide antigen of claim 77. The claim reads on a cell within a transgenic animal or a transgene therein given that the term "isolated" is not denoted in describing the nucleic acid.
With respect to the unisolated transgenes as “nucleic acids” of the instant claim discussed above, the state of the art at the time of filing was such that one of skill could not predict the phenotype of transgenics. The art of transgenic animals has for many years stated that the unpredictability lies, in part, with the site or sites of transgene integration into the target genome and that "the position effect" as well as unidentified control elements are recognized to cause aberrant expression of a transgene (Wall et Al., Theriogenology, Vol. 45, Pg. 57-68, 1996).
The elements of the particular construct used to make transgenic animals are also held to be critical, and they must be designed case by case without general rules to obtain good expression of a transgene; e.g., specific promoters, presence or absence of introns, etc. (Houdebine et Al., Journal of Biotechnology, Vol. 34, Pg. 269- 287, 1994). Furthermore, transgenic animals are regarded to have within their cells, cellular mechanisms that prevent expression of the transgene, such as methylation or deletion from the genome (Kappell et Al., Current Opinions in Biotechnology, Vol. 3, Pg. 548-553, 1992). Houdebine (Comparative Immunology, Microbiology, and Infectious Diseases, Vol. 32, Pg. 107-121, 2009) teaches progress has been made in the field of transgenic animals for production of foreign proteins (Abstract); however, constructing an efficient expression vector to produce a therapeutic protein is not a standard operation (Pg. 116, Paragraph, second). Therefore, undue experimentation is required to make and use a transgene and transgenic animal to produce the polypeptide of claim 77.
Examples in the literature aptly demonstrate that even closely related species carrying the same transgene construct can exhibit widely varying phenotypes. Mullins (1993, Hypertension, Vol. 22, No. 4, pp. 630-633) states that not all animals express a transgene sufficiently to provide a model for a disease as the integration of a transgene into different species of animal has been reported to give divergent phenotypes. For example, several animal models of human diseases have relied on transgenic rats when the development of mouse models was not feasible. Mullins (1990, Nature, Vol. 344, 541-544) produced outbred Sprague-Dawley x WKY rats with hypertension caused by expression of a mouse Ren-2 renin transgene. Hammer (1990, Cell, Vol. 63, 1099- 1112) describes spontaneous inflammatory disease in inbred Fischer and Lewis rats expressing human class I major histocompatibility allele HLA-B27 and human 02- microglobulin transgenes. Both investigations were preceded by the failure to develop human disease-like symptoms in transgenic mice expressing the same transgenes that successfully caused the desired symptoms in transgenic rats (Mullins, 1989, EMBO J., Vol. 8, pages 183-191). Thus, the use of nonmurine species for transgenesis will continue to reflect the suitability of a particular species for the specific questions being addressed, bearing in mind that a given construct may react very differently from one species to another.
The examiner notes here, in addition to these issues, even assuming arguendo a person having ordinary skill in the art could make a host organism with functional transgene that encodes the instantly recited SEQ ID NO: 3 or variants thereof, such as SEQ ID NO: 144, there is no predictability that the host will survive its expression. The transgene depends on the host for function and harm to the host, including death, renders the transgene nonfunctional and thus not enabled.
The art is well-aware of side effects caused by expressing proteins, such as therapeutic antibodies. In a transgenic cell or animal that expresses the same, an antibody will exert any possible side effect it can. It is not administered but chronically present and so such side effects are chronic and potentially more serious than any from an administered antibody. Hansel (Nature Reviews Drug Discovery, Vol. 9, Pg. 325-337, 2010) teaches in their table 1 on page 328 numerous exemplary side effects from licensed monoclonal antibodies to include: increased bleeding risk, infection, heart failure, cancer, thyroid disorder, autoimmune reactions, and cytokine release syndrome (CRS) to name only a few. One or more such effects, or similar, may occur with the polypeptide antigen instantly recited when administered and indeed be exacerbated by chronic exposure due to internal expression. For all these reasons, previously raised and new, transgenes are not enabled.
At the time of filing, the phenotype of a transgene and transgenic cell contained within any animal was unpredictable. The claims as written, encompassing a transgene in a transgenic animal, is not adequately described in the specification as to prevent excessive experimentation by the public to generate and use the invention. Applicants can obviate the instant rejection by amending the claim to recite the term "isolated" before the recitation, "nucleic acid" to specify they are not in a transgenic animal. Applicant may consider using purified in such claims if description is appropriate for such a term and it is not redefined away from standard meaning. Method claims using these products should also carry the appropriate adjectives above.
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to make and use transgenic animals possessing the claimed nucleic acid, with a reasonable expectation of success, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed nucleic acid, commensurate in scope with the claimed invention. The same can be said for the transgenes and transgenic animals encompassed by the instant claims. Thus, the claims are rejected here.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 77-80, 82-90, 92-94, 97-98, and 100 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a product of nature and natural phenomenon without significantly more.
The claims recite a polypeptide antigen comprising a SARS-CoV-2 S protein S1/S2 cut site or a S1/S’2 cute site, including the P3 peptide (SEQ ID NO: 3), a variant thereof, or a chemically modified form thereof (claim 77). The specification indicates that variants of the polynucleotides or polypeptides disclosed therein may have different degrees of sequence identity or similarity to said polynucleotides or polypeptides (spec., p. 20), and analogs or variants of peptides or polypeptides include those with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30 or more deletions, substitutions, or insertions of amino acid residues into a polypeptide, such as those disclosed herein (spec., p. 21).
Based on the variant language in the spec, the examiner is interpreting “ variant” to mean that SEQ ID NO: 144 is a variant of SEQ ID NO: 3. ABSS alignment (see below for a summary) shows that SEQ ID NO: 3 and SEQ ID NO: 144 have 25.1% sequence identity with a best local similarity of 70.4%.
This judicial exception is not integrated into a practical application because SEQ ID NO: 144 is identical to a portion of a SARS-CoV-2 spike sequence from a natural throat swab isolate (Genbank accession: QPZ33395.1, published 12/21/2020), as well as another SARS-CoV-2 spike protein sequence from a human host (NCBI Reference Sequence: YP_009724390.1, published 7/18/2020). See alignment below.
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Therefore, The claimed polypeptide antigen is a composition of matter (Step 1) and is drawn to a natural phenomenon, such as a naturally occurring SARS-CoV-2 spike protein (thereby rending the answer to Step 2A as yes). With regard to step 2B, Does the claim recite additional elements that integrate the judicial exception int a practical application?, the answer is no. The claimed invention is only drawn to a polypeptide antigen that comprises a naturally occurring amino acid sequence or the nucleic acid sequences that encodes this amino acid sequence. In addition, while the claimed invention also requires addition of a pharmaceutically acceptable carrier, water can function as such a carrier would not alter the structure or any of the properties of the claimed polypeptide antigen or nucleic acid sequence encoding said antigen.
The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception and do not amount to markedly different characteristics compared to the natural product. Furthermore, because the furin cut site or TMPRSS2 cut site is inherent to the peptide (claim 78), as Peacock et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312) discloses SARS-CoV-2 has a polybasic insertion (PRRAR) at the S1/S2 cleavage site that can be cleaved by furin (Peacock, Abstract). Additionally, a natural isolate would inherently possess a carrier in the form of saliva or other bodily fluid (claims 92 & 98), a SARS-CoV-2 virion naturally comprises two or more spike polypeptides (claim 93), and would induce humoral or cellular immunity against SARS-CoV-2 when administered to a subject, because it is foreign and would not be recognized as self (claim 94). Similarly, a SARS-CoV-2 virion would naturally encode the spike polypeptide (claim 97), and a natural SARS-CoV-2 isolate could reads on a vaccine (claim 100).
As pursuant to the Office's interpretation of the Myriad decision, a recitation of a naturally - occurring nucleic acid sequences that do not have a substantial or marked difference from the natural product is not patent eligible subject matter. Therefore, claims 77-80, 82-90, 92-94, 97-98, and 100 as written, read upon a naturally occurring SARS-CoV-2 polypeptides and nucleic acids that were found to have occurred naturally in nature without being subject to the "hand-of-person" and resulting in a substantial or markedly different product from that found in nature. Therefore, claim(s) 77-80, 82-90, 92-94, 97-98, and 100 do not recite eligible subject matter under 35 U.S.C. 101 in view of the Subject Matter Eligibility Test for Products and Processes, and the claimed invention is directed to non-statutory subject matter. This rejection is necessitated by expanded 35 USC §101 USPTO training in view of the USPTO's interpretation of Myriad. Applicant is directed towards the USPTO memos, which support the analysis of the claims; please review the latest materials regarding 35 USC §101 rejections.
Claim 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 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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 77-80 and 82-90 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Genbank accession: QPZ33395.1 (deposited 12/21/2020) as evidenced by Peacock, et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312).
The claims encompass a polypeptide antigen comprising a SARS-CoV-2 S protein S1/S2 cut site or a S1/S’2 cute site, including the P3 peptide (SEQ ID NO: 3), a variant thereof, or a chemically modified form thereof (claim 77, a representative claim).
The Prior Art
GenBank accession QPZ33395.1 (published 12/21/2020) discloses a partial surface glycoprotein amino acid sequence of SARS-CoV-2, isolated from a throat swab of an infected human (p. 1). QPZ33395.1 contains a fragment that is 100% identical in sequence to the instant SEQ ID NO: 144, see alignment below:
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The specification indicates that variants of the polynucleotides or polypeptides disclosed therein may have different degrees of sequence identity or similarity to said polynucleotides or polypeptides (spec., p. 20), and analogs or variants of peptides or polypeptides include those with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30 or more deletions, substitutions, or insertions of amino acid residues into a polypeptide, such as those disclosed herein (spec., p. 21).
Based on the variant language in the spec, the examiner is interpreting “ variant” to mean that SEQ ID NO: 144 is a variant of SEQ ID NO: 3. ABSS alignment (see below for a summary) shows that SEQ ID NO: 3 and SEQ ID NO: 144 have 25.1% sequence identity with a best local similarity of 70.4%.
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The furin cut site or TMPRSS2 cut site is inherent to the peptide disclosed by QPZ33395.1 (claim 78), as Peacock et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312) discloses SARS-CoV-2 has a polybasic insertion (PRRAR) at the S1/S2 cleavage site that can be cleaved by furin (Peacock, Abstract), which is present in QPZ33395.1.
Therefore, claims 77-80 and 82-90 are anticipated by Genbank accession: QPZ33395.1 as evidenced by Peacock, et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312).
Claims 77-80, 82-90, 92-94, 97-98, and 100 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Gershoni (WO2021205455A1, published 10/14/2021, priority date 4/7/2021) as evidenced by NCBI Reference Sequence: YP_009724390.1 (published 7/18/2020) and Peacock, et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312).
The claims encompass a polypeptide antigen comprising a SARS-CoV-2 S protein S1/S2 cut site or a S1/S’2 cute site, including the P3 peptide (SEQ ID NO: 3), a variant thereof, or a chemically modified form thereof (claim 77, a representative claim). An example of a variant of SEQ ID NO: 3 is SEQ ID NO: 144.
The Prior Art
Gershoni teaches methods and compositions related to vaccines and therapeutic compositions targeted at SARS-CoV-2 (Abstract). Gershoni discusses a SARS-CoV-2 spike protein sequence of YP_0097424390.1 (Gershoni SEQ ID NO: 6 is identical to the sequence of YP_0097424390.1), a portion of which is 100% identical to the instant SEQ ID NO: 144. Gershoni discloses another peptide, SEQ ID NO: 21, which is identical to the instant SEQ ID NO: 144, but lacks the 5’-terminal Glu residue. See ABSS sequence alignment below:
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YP_009724390.1 indicates that the amino acid sequence is a full-length conceptual translation obtained from Illumina sequencing (p. 1).
The specification indicates that variants of the polynucleotides or polypeptides disclosed therein may have different degrees of sequence identity or similarity to said polynucleotides or polypeptides (spec., p. 20), and analogs or variants of peptides or polypeptides include those with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30 or more deletions, substitutions, or insertions of amino acid residues into a polypeptide, such as those disclosed herein (spec., p. 21).
Based on the variant language in the spec, the examiner is interpreting “ variant” to mean that SEQ ID NO: 144 is a variant of SEQ ID NO: 3. ABSS alignment (see below for a summary) shows that SEQ ID NO: 3 and SEQ ID NO: 144 have 25.1% sequence identity with a best local similarity of 70.4%.
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The furin cut site or TMPRSS2 cut site is inherent to Gershoni’s SEQ ID NOs: 6 & 21 ( YP_009724390.1; claim 78), as Peacock et al. (Nat Microbiol. 2021 Jul;6(7):899-909. doi: 10.1038/s41564-021-00908-w. Epub 2021 Apr 27. PMID: 33907312) discloses SARS-CoV-2 has a polybasic insertion (PRRAR) at the S1/S2 cleavage site that can be cleaved by furin (Peacock, Abstract), which is present in Gershoni’s SEQ ID NOs: 6 and 21, and YP_00724390.1.
Gershoni also teaches that its compositions may comprise at least one pharmaceutically acceptable carrier, adjuvant, excipient, auxillary or diluent (p. 5;, p. 6 printout; claims). Gershoni discloses that dendrimers presenting multiple copies of any of the RBMs, RBDs, or spike proteins are encompassed by its disclosure, and tetrameric RBM may easily be produced by incorporating an Avitag sequence or any connecting moiety at the carboxyterminal end of any of the polypeptides of the invention, hence they will be C-terminally biotinylated (p. 76, para. 1). Additionally, the immune response generated by the immunogenic compositions of Gershoni may be in the form of a cellular or humoral response, or both (p. 85, printout p. 86). Gershoni also discloses a SARS-CoV-2 vaccine comprising a polypeptide that is an RBD or spike protein with a reconstituted RBM, any RBD or spike protein that comprises at least one linker that replaces an anchor loop or parts thereof, or a DNA or RNA vaccine that encodes any of the polypeptides disclosed in Gershoni (p. 85, printout p. 86).
Therefore, claims 77-80, 82-90, 92-94, 97-98, and 100 are anticipated by Gershoni as evidenced by NCBI Reference Sequence: YP_009724390.1 and Peacock, et al. .
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 77, 81 and 91 are rejected under 35 U.S.C. 103 as being unpatentable over Gershoni (supra) as evidenced by NCBI Reference Sequence: YP_009724390.1 (supra) and Peacock, et al. (supra) in view of Liu, et al. (Lancet. 2004 Mar 20;363(9413):938-47. doi: 10.1016/S0140-6736(04)15788-7. PMID: 15043961 ).
The Prior Art
The teachings of Gershoni, as evidenced by YP_009724390.1 (supra) and Peacock, et al. are described above. Gershoni also discloses C-terminally biotinylated receptor binding motifs (RBMs) of SARS-CoV-2 spike proteins (p. 76, para. 1). However, Gershoni does not teach SARS-CoV-2 spike proteins or peptides that are N-terminally biotinylated.
Liu teaches biotinylation of CP-1, a peptide derived from the heptad repeat 2 (HR2), and NP-1, a peptide derived from the heptad repeat 1 (HR1) region of SARS-CoV spike protein (p. 938, col. 1;Fig. 1; Table 1; p. 939, col. 2, paras. 2-4).
It would have been obvious to one of ordinary skill in the art to modify the SARS-CoV-2 spike proteins disclosed by Gershoni to be N-terminally biotinylated. Gershoni discloses biotinylation of SARS-CoV-2 RBMs at the C terminus, and N-terminal biotinylation of viral peptides, even SARS-CoV peptides, is known in the art, as taught by Liu. Accordingly, it would have been obvious to one of ordinary skill in the art to N-terminally biotinylate a SARS-CoV-2 S polypeptide antigen that comprises the instant SEQ ID NO: 144.
One of ordinary skill in the art would have been motivated to present multiple copies of SARS-CoV-2 spike peptides or proteins, or to label the peptides or proteins for other purposes known to be common in the art. There would be a reasonable expectation of success because Gershoni disclosed N-terminal biotinylation of SARS-CoV-2 spike proteins and peptides and Liu disclosed N-terminal biotinylation of SARS-CoV spike peptides. Therefore, claims 77-94, 97-98, and 100 were prima facie obvious before the priority date of the instant invention.
Allowable Subject Matter
SEQ ID NO: 3 is free of the prior art of record.
Conclusion
No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JEFFREY MARK SIFFORD whose telephone number is (571)272-7289. The examiner can normally be reached 8:30 a.m. - 5:30 p.m. ET with alternating Fridays off.
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/JEFFREY MARK SIFFORD/Examiner, Art Unit 1671 /BENJAMIN P BLUMEL/Primary Examiner, Art Unit 1671