DETAILED ACTION Non-Final Rejection Notice of Pre-AIA or AIA Status 1. 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 2. Applicant’s election of Group I claims 1-15 and 26 with and antibody species comprising heavy chain CDR sequences SEQ ID NOs: 11-13 and light chain CDR sequences SEQ ID NOs: 19-21 in the reply filed on 11/07/2025 is acknowledged. The elected antibody CDR sequences read on claims 1-12 and 26 that will be examined , and the claims 13-15 will be excluded from the examination in this office action although the claims belong to elected Group I. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Status of Claims 3 . Claims 1-15, 17, 19, 24 and 26 as filing list of 11/07/2025 are pending. 4. Claims 17, 19, and 24 are withdrawn due to Election/Restriction. 5. Claims 1-15 and 26 belong to Group I but only claims 1-12 and 26 read on the elected antibody species , and thus the Group I claims 13-15 will be excluded from the examination. 6. Claims 1-12 and 26 are under examination in this office action. Priority 7 . This application is a National Phase of International Application No. PCT/GB2021/050685, filed March 19, 2021, which designated the U.S., and that International Application was published under PCT Article 21(2) in English. This application also includes a claim of priority under 35 U.S.C. §119(a) and §365(b) to British patent application Numbers 2003980.6, filed March 19, 2020, and 2018582.3, filed November 26, 2020. The claim 3 that recite limitation on cross-neutralization of the claimed antibody or antigen binding fragment thereof with a function of cross-neutralizing all three claimed viruses SARS- CoV , MERS- CoV and SARS CoV-2 are eligible for priority date of 11/26/2020 because the copy of the application GB2018582.3 (on file) has support for the subject matter. The copy of the application GB2003980.6 (priority date 03/19/2020) does not have support for the cross-neutralizing antibody with all three claimed viruses SARS- CoV , MERS- CoV and SARS CoV-2. Information Disclosure Statement 8 . The information disclosure statement (IDS) submitted on 09/13/2022 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Objection s to Drawings 9 . The drawings are objected to because new corrected drawings in compliance with 37 CFR 1.121(d) are required in this application because multiple amino acid sequences alignment in Figures 10A, 10B, 12, 14D are not legible to read due to use of background used (See, Drawings filed on 09/13/2022). FILLIN "Enter appropriate reason" \* MERGEFORMAT Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be re - numbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Applicant is advised to employ the services of a competent patent draftsperson outside the Office, as the U.S. Patent and Trademark Office no longer prepares new drawings. The corrected drawings are required in reply to the Office action to avoid abandonment of the application. The requirement for corrected drawings will not be held in abeyance. Claim Objections 10 . Claims 8-11 are objected to because of the following informalities: It is not clear to which coronavirus (SARS- CoV , or MERS- CoV , or SARS-CoV-2) the claimed sequences in the SEQ ID NO belong to? Whether the claimed sequences are amino acid or nucleotide sequences. To bring in more clarity to the claims without the requirement to refer the specification, applicant may amend the claims 8-11. Appropriate correction is required. Claim Rejections - 35 USC § 112 11. 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 s 5-11 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. The term “substantially” in claim 5-7, 10 and 11, and “variants” in claims 8- 9 are relative term s which render the claim s indefinite. The terms “substantially” or “variants” is not defined by the claim, nor does the specification provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. Claims 5-7, 10 and 11 recites “ substantially as set out in SEQ ID NO: …” Substantially, is a “relative term” which is neither defined, nor exemplified in the specification accordingly there is no standard for the degree of variability (e.g. changes: deletion/addition/subtraction) of amino acid sequence. See, MPEP §§ 2173.05(b) . Claims 8 and 9 recites the term “variants” for the claimed sequences of antibody or fragments thereof which is neither defined, nor exemplified in the specification accordingly there is no standard for the degree of variability (e.g. changes: deletion/addition/subtraction) of amino acid sequence. See, See, MPEP §§ 2173.05(b). Claim Rejections - 35 USC § 112 1 2 . The following is a quotation of 35 U.S.C. 112(d): (d) REFERENCE IN DEPENDENT FORMS.— Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph: Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. Claims 2-6, and 8-11 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends , or for failing to include all the limitations of the claim upon which it depends. The claim 1 is interpreted to be directed to an antibody or antigen binding fragment thereof that binds to S2 domain of SARS-CoV-2 virus , b ecause in claim 1 line 3 “and/or” is used to separate the limitations. The claims 2-6, and 8-11 dependent on claim 1 recites cross-reactivity of the antibody of claim 1 with SARS- CoV and MERS- CoV and SARS-CoV-2 and thus failed to further limit the subject matter of the claim 1 upon which claims 2-6, and 8-11 depends. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. Claim Rejections - 35 USC § 112 1 3 . 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 1-12 and 26 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 1-12 and 26 are interpreted (see, claim 1 interpretation) to be directed to an alternative claim limitation, an antibody or polyclonal antibody ( the instant specification (02/16/2023) page 19 of 77, line 6, recites an antibody as a polyclonal antibody) that binds to the spike protein S2 domain of SARS-CoV-2 virus. Thus, the instant claims 1-12 and 26 (the instant claims 2-12 and 26 are dependent on claim 1) as interpreted or reads on to comprise an alternative limitation an antibody or antigen-binding fragment thereof that binds to the spike protein S2 domain of SARS CoV-2 virus are directed to a genus of antibody. The full s c ope of the claims 8 and 9 is not clear because the claims recite the term “variants” for the claimed sequences of antibody or fragments thereof which is neither defined, nor exemplified in the specification accordingly there is no standard for the degree of variability (e.g. changes: deletion/addition/subtraction) of amino acid sequence. The full scope of the claims 5-7, 10 and 11 is not clear because t he claims recite “substantially ” as set out in SEQ ID NO: …” with regard to the SARS-CoV-2 viral S2 subunit protein sequences. “ Substantially ” , is a “relative term” which is neither defined, nor exemplified in the specification accordingly there is no standard for the degree of variability (e.g. changes: deletion/addition/subtraction) of amino acid sequence. To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba , B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar , 935 F.2d at 1563, 19 USPQ2d at 1116. The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice (see i )(A) above), reduction to drawings (see i )(B) above), or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus (see i )(C) above). See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. See Juno Therapeutics, Inc. v. Kite Pharma, Inc., 10 F.4th 1330, 1337, 2021 USPQ2d 893 (Fed. Cir. 2021). See MPEP 2163 “Written Description Guidelines”. 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). The issue is whether the skilled artisan would understand inventor to have invented, and been in possession of, the invention as claimed. The Federal Circuit has clarified the application of the written description requirement to inventions in the field of biotechnology. See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568,43 USPQ2d l398, 1406 (Fed. Cir. 1997). The Court stated that a written description of an invention requires a precise definition, one that defines the structural features of the chemical genus that distinguishes it from other chemical structures. A definition by function does not suffice to define the genus because it is only an indication of what the genus does, rather than what it is. Further, the Court held that to adequately describe a claimed genus, an applicant must describe a representative number of species of the claimed genus, and that one of skill in the art should be able to “visualize or recognize the identity of the members of the genus.” Amgen Inc. vs Sanofi (2017-1480, Fed Cir, 2017) states that "an adequate written description must contain enough information about the actual makeup of the claim products - a precise definition such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other material," which may be present in "function "terminology "when the art has established a correlation between structure and function" (page 17,1st paragraph). The claims 8 and 9 recite the term “variants” for the claimed sequences of antibody or fragments thereof which is neither defined, nor exemplified in the specification accordingly there is no standard for the degree of variability (e.g. changes: deletion/addition/subtraction) of amino acid sequence. It has been well known in the art that minor structural differences even among structurally related compounds or compositions can result in substantially different biological or pharmacological activities. It is known in the art that the substitution of amino acids within the protein sequence may cause the loss of function of the protein. Thus, the large number of sequences (“ variant” antibody or fragments) encompassed by the current claims may or may not be effective in achieving the binding affinities of the claims. Specifically in relation to CDRs, it should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin ( Janeway et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. The structure of a typical antibody molecule. Available from: ncbi.nlm.nih.gov/books/NBK27144/. See entire article). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody ( Rudikoff et al. Single amino acid substitution altering antigen-binding specificity. Proc Natl Acad Sci U S A. 1982;79(6):1979-1983, see entire article, particularly the abstract and the middle of the left column of page 1982). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves. The claims 1-12 and 26 also encompass alternative limitation an antigen-binding fragment thereof (read on an antigen-binding fragment of the antibody). The claim 12 recite antibody VH and VL CDR sequences (SEQ ID NO), individual CDR-H1-H3 and CDR-L1-L3. For example , the instant claim 12 is recited/claimed as: Claim 12. The antibody or antigen-binding fragment thereof according to claim 1 , wherein the antibody or antigen-binding fragment thereof comprises a CDR-H1 domain comprising SEQ ID No: 11, a CDR-H2 domain comprising SEQ ID No: 12, a CDR-H3 domain comprising SEQ ID No: 13, a CDR-L1 domain comprising SEQ ID No: 19, a CDR-L2 domain comprising SEQ ID No: 20, and/or a CDR-L3 domain comprising SEQ ID No: 21, optionally wherein the antibody or antigen-binding fragment thereof comprises at least one , at least two, at least three, at least four, at least five, or at least six of the CDRs. The instant specification does not have written description support by example to demonstrate that only one of the six CDRs would bind to the spike protein S2 domain of SARS-CoV-2 or S2 domain of both SARS-CoV-2 and SARS- CoV or S2 domain of all three SARS-CoV-2, MERS- CoV and SARS- CoV with a dissociation equilibrium constant (KD value) as that of a complete antibody constructed from all three claimed heavy chain CDR sequence and three claimed light chain CDR sequence. The ordinary skill in the art is not reasonably convinced how any one of the three heavy chain CDR 1-3 and any one of the three light chain CDR 1-3 can be combined to form a functional molecule that bind to the spike protein S2 domain of the claimed coronaviruses with a similar dissociation equilibrium constant (KD value) as that of a complete antibody. The instant claim 3 (depends from claim 1) also encompass cross-neutralization of the claimed SARS- CoV , MERS- CoV and SARS CoV 2 as a function of the antibody or antigen-binding fragment thereof according to claim 1. Multiple combinations of CDRs are possible and can be envisioned by the ordinary skills. The ordinary skill is not convinced that all the CDR combination or a single CDR would have a function of binding to the spike protein S2 domain of the claimed coronaviruses at the same affinity as that of the binding of a complete natural antibody directed to bind to the S2 domain and also would less likely have similar dissociation equilibrium constant (KD value) and that would affect the binding or neutralization of the claimed coronaviruses affecting the derived diagnostic assay kit performance or therapeutic treatment of the claimed coronavirus infected subject. Therefore, the ordinary skill in the art is not reasonably convinced that the applicant and inventors at the time the application was filed, had possession of the claimed invention since there is insufficient representative species and/or identifying characteristics to place applicant in possession of the generic scope of the claimed invention. Claim Rejections - 35 USC § 101 1 4 . 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. Note 1: For compact prosecution purpose the claims 2-4 (dependent on claim 1 are interpreted to inherit “and/or” claim limitation, and therefore the claims 2-4 are interpreted to read on binding or reactive or neutralizing to SARS-CoV-2 virus only or SARS-CoV2 virus and SARS- CoV virus. Note 2: The claims comprising subject matter regarding an antibody neutralizing SARS-CoV-2 is eligible for priority date of 11/26/2020 filing of foreign application GB2018582.3 because the SARS-CoV-2 neutralizing antibodies are disclosed in foreign application GB2018582.3. Claims 1-4 are rejected under 35 U.S.C. 101 because the claims are interpreted to be directed to a polyclonal antibody (See, instant Specification (02/16/2023) page 19 of 77, line 6). Lv et al 2020 (Cell Reports 31, 107725, 2 June 2020) is directed to screening of plasma from SARS CoV-2 virus infected patient (COVID-19 patients) and in SARS- CoV infected patients for presence of cross - neutralizing or cross-reactive antibodies in the plasma against coronaviruses SARS-CoV-2 and SARS- CoV . Lv et al 2020 disclosed presence of SARS-CoV-2 S2 subunit binding antibodies in the plasma of naturally infected SARS-CoV-2 COVID-19 patients and SARS- CoV infected patients (See, page 2, col 2 legends to Figure 1-B). SARS-CoV-2 and SARS- CoV cross-neutralizing antibodies were disclosed in the plasma of patients infected with SARS-CoV-2 or SARS- CoV (See, page 2, col 2 legends to Figure 1-C). Therefore, the polyclonal antibodies directed to and that binds to S2 subunit of SARS-CoV-2 are found in nature in SARS CoV-2 or SARS- CoV infected people. Similarly, the plasma comprising polyclonal antibodies directed to S2 subunit of SARS-CoV-2 or SARS- CoV that are neutralizing are found in nature in SARS CoV-2 or SARS- CoV infected people. Additionally, Zhu et al 2020 teaches cross-reactive neutralization of SARS-CoV-2 by serum antibodies from recovered SARS patients and immunized animals. To investigate the effects of previous SARS- CoV infection on the ability to recognize and neutralize SARS-CoV-2, we analyzed 20 convalescent serum samples collected from individuals infected with SARS- CoV during the 2003 SARS outbreak. All patient sera reacted strongly with the S1 subunit and receptor binding domain (RBD) of SARS- CoV ; cross-reacted with the S ectodomain, S1, RBD, and S2 proteins of SARS-CoV-2 ; and neutralized both SARS- CoV and SARS-CoV-2 S protein–driven infections (See, abstract). Fig 1 C shows reactivity of convalescent SARS sera with the ………. and S2 proteins of SARS-CoV-2 . Thus, claims 1-4 are rejected under 35 U.S.C. 101 as recited supra . Claim Interpretation 1 5 . The claims in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be understood by one of ordinary skill in the art. Claim 1. The instant claim 1 is interpreted to be directed to an antibody or antigen-binding fragment thereof that binds to the spike protein S2 domain of severe acute respiratory syndrome coronavirus (SARS- CoV ), Middle East respiratory syndrome-related coronavirus (MERS- CoV ) and/ or severe acute respiratory syndrome coronavirus 2 (SARS CoV-2). An antibody is interpreted to be a polyclonal antibody from human or animal model. An antibody or polyclonal antibody can be derived from a natural infection of a human or animal with a SARS CoV-2 virus and an antibody or polyclonal antibody can bind to S2 protein of SARS-CoV-2 virus. An antibody is interpreted to be a monoclonal antibody of human or mouse or animal model. An antibody is interpreted to comprise one or more CDRs of the light chain and heavy chain of an antibody. An antibody or antigen-binding fragment thereof is interpreted to binds to the spike protein S2 domain of SARS CoV-2. An antibody or antigen-binding fragment thereof that binds to the spike protein S2 domain of SARS- CoV , and MERS- CoV . An antibody or antigen-binding fragment thereof that binds to the spike protein S2 domain of SARS- CoV , MERS- CoV and SARS CoV-2. Claim 12: The instant claim 12 (dependent on claim 1) is interpreted to be directed to the antibody or antigen-binding fragment thereof comprises a CDR-H1 domain comprising SEQ ID No: 11, a CDR-H2 domain comprising SEQ ID No: 12, a CDR-H3 domain comprising SEQ ID No: 13, a CDR-L1 domain comprising SEQ ID No: 19, a CDR-L2 domain comprising SEQ ID No: 20, and/or a CDR-L3 domain comprising SEQ ID No: 21. Alternatively, as recited optionally in the claim 12, the claim is interpreted to be directed to the antibody or antigen-binding fragment thereof that binds to the spike S2 domain of the virus and comprises at least one , at least two, at least three, at least four, at least five, or at least six of the CDRs. Claim Rejections - 35 USC § 102 1 6 . 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. Claim s 1 and 4 are rejected under 35 U.S.C. 102“(a)(1)” as being anticipated by Zheng et al 2020 ( bioRxiv preprint doi : https://doi.org/10.1101/2020.03.06.980037; this version posted March 7, 2020). Claim 1: Zheng et al 2020 anticipated claim 1 by disclos ing four mu r ine monoclonal antibod ies (2B2, 1A9, 4B12 and 1G10) raised S2 subunit of spike protein of SARS CoV (S amino acid 1029-1192) that cross-reacted in western blot (Fig 1A) and immunofluorescence assay (Fig 2B) with amino acids 1048 to 1206 of the S protein of SARS-CoV-2. The mAb 1A9 reacted SARS-CoV-2 infected cells (Fig 4), (See, abstract, page 9, entire article). Claim 4: Zheng et al 2020 anticipated claim 4 limitation (ii) by dislosing an antibody, a monoclonal antibody ( mAb 1A9) binds to the spike protein S2 domain of SARS- CoV and SARS CoV2 (See, abstract, Fig 1A, Fig 2B, Fig 4, page 9, entire article). Claim Rejections - 35 USC § 103 1 7 . 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. 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. 1 8 . Claims 1-4 are rejected under 35 U.S.C. 103 as being unpatentable over Zheng et al 2020 ( bioRxiv doi.org/10.1101/2020.03.06.980037; 03/7/2020) and further in view of Lv et al 2020 (Cell Reports 31, 107725, 2 June 2020), and Zhu et al 2020 (Sci Adv. 2020 Nov 6;6(45): eabc 9999). Claims 1-4: The disclosures of Zheng et al 2020 as applied to claims 1-4 recited above under 35 U.S.C. 102 (a)(1) are incorporated here in entirety to render obvious the claims 1-4 under 35 U.S.C. 103. Additionally, Lv et al 2020 is directed to screening of plasma from SARS CoV-2 virus infected patient (COVID-19 patients) and in SARS- CoV infected patients for presence of cross-neutralizing or cross-reactive antibodies in the plasma against coronaviruses SARS-CoV-2 and SARS- CoV . Lv et al 2020 disclosed presence of SARS-CoV-2 S2 subunit binding antibodies in the plasma of naturally infected SARS-CoV-2 COVID-19 patients and SARS- CoV infected patients (See, page 2, col 2 legends to Figure 1-B). SARS-CoV-2 and SARS- CoV cross-neutralizing antibodies were disclosed in the plasma of patients infected with SARS-CoV-2 or SARS- CoV (See, page 2, col 2 legends to Figure 1-C). Therefore, the polyclonal antibodies directed to and that binds to S2 subunit of SARS-CoV-2 are found in nature in SARS CoV-2 or SARS- CoV infected people. Similarly, the plasma comprising polyclonal antibodies directed to S2 subunit of SARS-CoV-2 or SARS- CoV that are neutralizing are found in nature in SARS CoV-2 or SARS- CoV infected people. Additionally, Zhu et al 2020 teaches cross-reactive neutralization of SARS-CoV-2 by serum antibodies from recovered SARS patients and immunized animals. To investigate the effects of previous SARS- CoV infection on the ability to recognize and neutralize SARS-CoV-2, we analyzed 20 convalescent serum samples collected from individuals infected with SARS- CoV during the 2003 SARS outbreak. All patient sera reacted strongly with the S1 subunit and receptor binding domain (RBD) of SARS- CoV ; cross-reacted with the S ectodomain, S1, RBD, and S2 proteins of SARS-CoV-2 ; and neutralized both SARS- CoV and SARS-CoV-2 S protein–driven infections (See, abstract). Fig 1 C shows reactivity of convalescent SARS sera with the ………. and S2 proteins of SARS-CoV-2 . It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art teaching of Zheng et al 2020 by incorporating additional teachings of Zheng et al 2020 on conserved amino acid sequences in S2 domain of the claimed coronaviruses, and disclosures of Lv et al 2020 and Zhu et al 2020 on presence of the S2 subunit protein reactive and cross neutralizing antibodies in plasma of patients infected with SARS- CoV or SARS-CoV-2 to arrive at the inventions of claims 1-4. Lv et al 2020 and Zhu et al 2020 provides t he motivation for the S2 subunit protein reactive antibodies, the motivation would have been useful to develop or generate broadly cross-reactive or cross-neutralizing mAbs against epitopes or antigenic regions within the S2 subunit of Spike protein that would bind or neutralize SARS-CoV-2, SARS CoV and MERS- CoV to develop diagnostic kit or mAb based therapeutics for commercial success. There would have been a reasonable expectation of success given the applied prior arts and required laboratory skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the invention as claimed in claims 1-4. See KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) (see MPEP § 2143, example of rationales, A-G). 1 9 . Claims 5-11 are rejected under 35 U.S.C. 103 as being unpatentable over combined teachings of Zheng et al 2020 ( bioRxiv doi.org/10.1101/2020.03.06.980037; 03/7/2020) , Lv et al 2020 (Cell Reports 31, 107725, 2 June 2020), and Zhu et al 2020 (Sci Adv. 2020 Nov 6;6(45): eabc 9999) as applied to claims 1-4 above, and further in view of Liu et al 2020 (J Med Virol . 2020 Jun;92(6):595-601) , Elshabrawy et al 2012 ( PLoS One. 2012;7(11 ):e 50366), Miyoshi-Akiyama et al 2011 (J Infect Dis. 2011 Jun 1;203(11):1574-81), Duan et al 2005 ( Biochem Biophys Res Commun . 2005 Jul 22;333(1):186-93), Leung et al 2006 (WO2006095180A2 , 09/14/ 2006) . Claims 5-11 : The combined prior art teachings of Zheng et al 2020 , Leung et al 2006, and Zhu et al 2020 as recited supra renders obvious claims 1-4 . However, does not explicitly teach the added limitations of instant claims 5-11. Zheng et al 2020 additionally teaches that an immunogenic domain in the S2 subunit of SARS- CoV S is highly conserved in multiple strains of SARS-CoV-2 virus (See, abstract). Liu et al 2020 teaches structural diagrams of spike glycoproteins of SARS‐ CoV , MERS‐ CoV , and SARS‐CoV‐2. All spike proteins of coronaviruses contain S1 subunit and S2 subunit , which were divided by the S cleavage sites. FP, fusion peptide; HR, heptad repeat 1 and heptad repeat 2 ; RBD, receptor‐binding domain, contains core binding motif in the external subdomain; SP, signal peptide (See, page 596 Fig 1, entire article). Elshabrawy et al 2012 teaches human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS- CoV spike protein are more broadly neutralizing. Further, many human Mabs that neutralize or bind to S2 domain (HR1 and HR2) of SARS- CoV are disclosed in Table 1 on page 7). Miyoshi-Akiyama et al 2011 discloses neutralizing antibody 5H10 binding to aa 791-805 in the S2 domain of SARS- CoV spike protein , a region which is homologous between SARS- CoV , MERS and SARS-CoV-2 (See, page 1576 col 2 para 2). Duan et al 2005 discloses neutralizing antibodies binding a mino acid 1023-1189 in the S2 domain in the SARS- CoV spike protein (See, page 191, col 1, para 1). Leung et al 2006 (WO2006095180A2) discloses an antibody that binds to amino acid 803-828 of S2 domain of SARS spike protein (See, page 5, para 3, page 11 para 1). Lv et al 2020 is directed to screening of plasma from SARS CoV-2 virus infected patient (COVID-19 patients) and in SARS- CoV infected patients for presence of cross-neutralizing or cross-reactive antibodies in the plasma against coronaviruses SARS-CoV-2 and SARS- CoV . Lv et al 2020 disclosed presence of SARS-CoV-2 S2 subunit binding antibodies in the plasma of naturally infected SARS-CoV-2 COVID-19 patients and SARS- CoV infected patients (See, page 2, col 2 legends to Figure 1-B). SARS-CoV-2 and SARS- CoV cross-neutralizing antibodies were disclosed in the plasma of patients infected with SARS-CoV-2 or SARS- CoV (See, page 2, col 2 legends to Figure 1-C). Therefore, the polyclonal antibodies directed to and that binds to S2 subunit of SARS-CoV-2 are found in nature in SARS CoV-2 or SARS- CoV infected people. Similarly, the plasma comprising polyclonal antibodies directed to S2 subunit of SARS-CoV-2 or SARS- CoV that are neutralizing are found in nature in SARS CoV-2 or SARS- CoV infected people. Zhu et al 2020 teaches cross-reactive neutralization of SARS-CoV-2 by serum antibodies from recovered SARS patients and immunized animals. To investigate the effects of previous SARS- CoV infection on the ability to recognize and neutralize SARS-CoV-2, we analyzed 20 convalescent serum samples collected from individuals infected with SARS- CoV during the 2003 SARS outbreak. All patient sera reacted strongly with the S1 subunit and receptor binding domain (RBD) of SARS- CoV ; cross-reacted with the S ectodomain, S1, RBD, and S2 proteins of SARS-CoV-2 ; and neutralized both SARS- CoV and SARS-CoV-2 S protein–driven infections (See, abstract). Fig 1 C shows reactivity of convalescent SARS sera with the ………. and S2 proteins of SARS-CoV-2 . The SARS CoV-2 virus (Wu et al 2019, Nature 579 (7798), 265-269 (2020), Genbank accession number NC_045512, Protein id YP_009724390.1) , MERS CoV virus ( Shirato et al 2019, Front Microbiol 10, 1326 (2019), GenBank: QBM11737.1, protein id MK564474.1), and SARS CoV virus (Wu et al 2009, Genomics Proteomics Bioinformatics 1 (2), 131-144 (2003), SARS- CoV , GenBank Accession AY278488, protein i d AAP30030.1) S2 subunit amino acids sequences , and variant sequences as claimed in claims 5-11 are known in the art. Therefore, the S2 subunit protein binding antibody or antigen binding fragment thereof as taught by the prior art above including polyclonal antibodies from the plasma being broadly cross-reactive to the S2 protein are reasonably expected to bind or cross-react to the claimed amino acid sequences recited in the SEQ ID NO s of in instant claims 5-11. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art teaching of Zheng et al 2020 by incorporating additional teachings of Zheng et al 2020 and Liu et al 2020 on conserved amino acid sequences in S2 domain of the claimed coronaviruses, and disclosures of Elshabrawy et al 2012, Miyoshi-Akiyama et al 2011, Duan et al 2005, Leung et al 2006 on mAbs that bind to the epitope or antigenic regions within conserved S2 subunit, and disclosure of both Lv et al 2020 and Zhu et al 2020 on SARS CoV or SARS-CoV-2 infected human patients and finding of the presence in plasma of the cross-reactive antibodies that bind to S2 subunit and cross-neutralizing antibodies to the SARS CoV or SARS-CoV-2 to arrive at the inventions of claims 5-11. The motivation would be to develop or generate broadly cross-reactive or cross-neutralizing mAbs against epitopes or antigenic regions within the S2 subunit of Spike protein that would bind or neutralize SARS-CoV-2 , SARS CoV and MERS- CoV to develop diagnostic kit or mAb based therapeutic s for commercial success. There would have been a reasonable expectation of success given the applied prior arts and required laboratory skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the invention as claimed in claims 5-11 . See KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) (see MPEP § 2143, example of rationales, A - G). 20 . Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Zheng et al 2020 ( bioRxiv doi.org/10.1101/2020.03.06.980037; 03/7/2020) , Lv et al 2020 (Cell Reports 31, 107725, 2 June 2020), and Zhu et al 2020 (Sci Adv. 2020 Nov 6;6(45): eabc 9999) as applied to claims 1-4 above, and further in view of Kang et al 2011 (US7951370B2, 05/31/2011), Bombardieri et al 2020 (US10590188B2, 03/17/2020), Kahnert et al 2015 ( US 20150259433A1, 09/17/2015), Papadopoulos et al 2011 (US7919593B2, 04/05/2011), Stevens et al 2009 (US7605237B2, 10/20/2009), Robbiani 2019 (US10196438B2, 02/05/2019) , Ngo 2020 (US10858443B2, 12/08/2020; with an earlier priority to US20180346589A1 published 12/06/2018), and Weinstock 2009 (US7504490B1, 03/17/2009) . Claim 12. The antibody or antigen-binding fragment thereof according to claim 1, wherein the antibody or antigen-binding fragment thereof comprises a CDR-H1 domain comprising SEQ ID No: 11, a CDR-H2 domain comprising SEQ ID No: 12, a CDR-H3 domain comprising SEQ ID No: 13, a CDR-L1 domain comprising SEQ ID No: 19, a CDR-L2 domain comprising SEQ ID No: 20, and/or a CDR-L3 domain comprising SEQ ID No: 21, optionally wherein the antibody or antigen-binding fragment thereof comprises at least one , at least two, at least three, at least four, at least five, or at least six of the CDRs. Regarding Claims 12: Zheng et al 2020 as recited supra teaches claims 1, however, does not teach the antibody defined by the CDR sequences. The claim 12 has two alternative interpret ations: The claimed antibody comprises all six claimed CDR sequences CDR-H1-H3 in SEQ ID NO: 11-13 and CDR-L1-L3 in SEQ ID NO: 19-21, or The claimed antibody requires at least one of the six claimed CDR sequences CDR-H1-H3 in SEQ ID NO: 11-13 and CDR-L1-L3 in SEQ ID NO: 19-21. ( i ) The Prior Art Teachings for: The claimed antibody comprises all six claimed CDR sequences CDR-H1-H3 in SEQ ID NO: 11-13 and CDR-L1-L3 in SEQ ID NO: 19-21: Ngo 2020 (US10858443B2, 12/08/2020; with an earlier priority to US20180346589A1 published 12/06/2018) disclosed SEQ ID NO. 29 (Db) that has only one instant SEQ ID NO: 11 CDR-H1 with 100% amino acid match. However, the searched claimed antibody Heavy chain comprising CDR-H1-H3 SEQ ID NOs: 11-13 is free of prior art because there is only 51% amino acid sequence identity match available with an antibody sequence from which all three CDR-H1-H3 are derived in the prior art sequences of the record based on the USPTO STIC sequence search. Query Match 51.5 %; Score 88.5; Length 248; Best Local Similarity 25.9%; Matches 22; Conservative 2; Mismatches 6; Indels 55; Gaps 2; Qy 1 GYTFTSYA-----------------INAGNGNT--------------------------- 16 |||||||| :||||||| Db 27 GYTFTSYAMHWVRQAPGQRLEWMGWMNAGNGNTKYSQKFQGRVTITRDTSASTAYMELSS 86 Qy 17 -----------ARDRHMVVPAAVFD 30 |||| :|| | Db 87 LRSEDTAVYYCARDRVPTIPAYRID 111 Weinstock 2009 (US7504490B1, 03/17/2009) disclosed SEQ ID NO. 33971 (Db) that has only 60% identity with instant heavy chain CDR-L1-L3 SEQ ID NOs: 19-21. The searched claimed antibody Light chain comprising CDR-L1-L3 is free of prior art as there is only 60% amino acid sequence identity match available with an antibody sequence from which all three CDR-L1-L3 sequences are derived in the prior art sequences of the record based on the USPTO STIC sequence search. Query Match 60.3 %; Score 44; Length 180; Best Local Similarity 61.5%; Matches 8; Conservative 3; Mismatches 2; Indels 0; Gaps 0; Qy 2 SISSWKASQQYGT 14 |:|||:|| : || Db 29 SVSSWEASMRPGT 41 (ii) The Prior Art Teachings for: The claimed antibody requires at least one of the six claimed CDR sequences CDR-H1-H3 in SEQ ID NO: 11-13 and CDR-L1-L3 in SEQ ID NO: 19-21. Kang et al 20 11 (US7951370B2, 05/31/2011) teaches SEQ ID NO: 1 that has 100% identity to SEQ ID NO: 11 Qy 1 GYTFTSYA 8 |||||||| Db 1 GYTFTSYA 8 Bombardieri et al 2020 (US10590188B2, 03/17/2020, with a priority to US20170129948A1 published on 11/05/2017) teaches SEQ ID NO: 108 that has 100% identity to SEQ ID NO: 12. Qy 1 INAGNGNT 8 |||||||| Db 1 INAGNGNT 8 Kahnert et al 2015 (20150259433A1, 09/17/2015) teaches SEQ ID NO: 10 that has 100% identity to SEQ ID NO: 12. Qy 1 GYTFTSYA 8 |||||||| Db 1 GYTFTSYA 8 Papadopoulos et al 2011 (US7919593B2, 04/05/2011) disclosed SEQ ID NO: 190 teaches instant SEQ ID NO: 19. Qy 1 QSISSW 6 |||||| Db 1 QSISSW 6 Stevens et al 200 9 (US7605237B2, 10/20/2009) teaches SEQ ID NO: 319 that has 100% identity with instant SEQ ID NO: 20. Qy 1 KAS 3 ||| Db 1 KAS 3 Robbiani 2019 (US10196438B2, 02/05/2019) teaches SEQ ID NO: 24 that has 100% identity with instant SEQ ID NO: 21. Qy 1 QQYGT 5 ||||| Db 2 QQYGT 6 The heavy and light chain CDR sequences are derived from different antibodies from different prior arts. However, the claim is directed to require at least one of the six CDR sequence, and the prior art taught CDR sequences satisfy the requirement although the prior arts are not directed to coronavirus antibody. The CDR sequence is available and taught by the prior art and is reasonably expected to perform the function of binding to S2 subunit of SARS- CoV , MERS- CoV and SARS-CoV-2. Therefore, i t would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art teaching of Zheng et al 2020 by incorporating additional teachings on the claimed antibody CDR sequences taught by Kang et al 2011 (SEQ ID NO: 11) , Bombardieri et al 2020 (SEQ ID NO: 12) , Kahnert et al 2015 (SEQ ID NO: 13) , Papadopoulos et al 2011 (SEQ ID NO: 19) , Stevens et al 2009 (SEQ ID NO: 20) , and Robbiani 2019 (SEQ ID NO: 21) and combine the applied prior art antibody CDR sequences for one or more or all six CDRs with the required antibody framework to develop cross-reactive antibody that bind to the S2 subunit of Spike protein of SARS-CoV-2, SARS CoV and MERS- CoV to develop a diagnostic kit or therapeutics and for commercial success. There would have been a reasonable expectation of success given the applied prior arts and required laboratory skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the invention as claimed in claim 12. See KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) (see MPEP § 2143, example of rationales, A-G). 2 1 . Claim 26 is rejected under 35 U.S.C. 103 as being unpatentable over Zheng et al 2020 ( bioRxiv doi.org/10.1101/2020.03.06.980037; 03/7/2020) , Lv et al 2020 (Cell Reports 31, 107725, 2 June 2020), and Zhu et al 2020 (Sci Adv. 2020 Nov 6;6(45): eabc 9999) as applied to claims 1-4 above, and further in view of Pan et al 2020 (The Lancet Infectious Diseases, published online 02/24/2020, Volume 20, Issue 4, 2020, Pages 411-412) , and Chen et al 2020 ( Emerg Microbes Infect. 2015 Apr;4(4 ):e 26), and Mizuike et al 2011 (Clin Vaccine Immunol. 2011 Mar;18(3):494-9). Zheng et al 2020 as recited supra renders obvious claims 1-4. Zheng et al 2020 does not teach a subject suffering from SARS-CoV-2 coronavirus infection and a sample type and collection of a clinical specimen for detection of the viral antigen. Pan et al 2020 teaches collection of clinical specimens, throat swabs and sputum for detection of SARS-CoV2 viral antigen in a diagnostic test, and the viral load in the samples (See, entire article, Figure). Zheng et al 2020 additionally teaches the disclosed S2 binding cross-reactive mAbs may serve as tools useful for SARS-CoV-2 research as well as for the development of diagnostic assays for coronavirus disease COVID-19 (See, abstract). Chen et al 2020 teaches a sensitive and specific antigen detection assay for Middle East respiratory syndrome coronavirus . Further refinement of the test and the development of a rapid antigen detection kit for on-the-spot diagnosis are warranted (See, abstract , page 5, col 1 last para ) . Mizuike et al 2011 is in the virology art , a respiratory virus and teaches development of two types of rapid diagnostic test kits to detect the hemagglutinin or nucleoprotein of the swine-origin pandemic influenza A virus H1N1 (See, abstract, entire article , Fig. 3 ). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art teaching of Zheng et al 2020 by incorporating additional teachings of Zheng et al 2020 on motivation for development of diagnostic assays for coronavirus disease COVID-19 by using the Zheng et al 2020 prior art disclosed cross-reactive antibodies, and teachings of Pan et al 2020 on specimen collection from suspected or confirmed SARS-CoV-2 infected COVID-19 patients, and Chen et al 2020 on a method for development of a diagnostic kit for MERS- CoV antigen detection, and Mizuike et al 2011 on a method for development of influenza antigen diagnostic kit and the diagnostic evaluation of the kit to arrive at the invention of claim 26 . The motivation would be to develop a broadly reactive coronavirus antigen detection diagnostic kit by using the taught cross-reactive mAbs to detect the S2 subunit of Spike protein of SARS-CoV-2, SARS CoV and MERS- CoV in a clinical specimen and for commercial success. There would have been a reasonable expectation of success given the applied prior arts and required laboratory skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, or motivation in the prior art that would