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 without traverse of Group I claims 1-15 and 24 in the reply filed on 02/09/2026 is acknowledged.
The Group I is modified to include claim 16 in view of applicant’s response.
The modified Group I comprise claims 1-16 and 24.
The elected species without traverse are VH SEQ ID NO: 25 and VL SEQ ID NO: 29 (claim 1). The applicant has clarified that the election of species VH SEQ ID NO: 25 and VL SEQ ID NO: 29 (claim 1) comprise heavy and light chain CDR sequences SEQ ID NO: 26-28, and SEQ ID NO: 30-32 (claim 2).
Claim 24: Applicant elected without traverse a species antibody, antigen binding fragment.
The unelected groups Group II (claims 17-18), Group III (claims 19-23), Group IV (claim 25), modified Group V (claims 26-27), and Group VI (claims 28-29 and 32) are withdrawn from examination due to Restriction/Election.
The Restriction/Election of species without traverse is made final.
Markush Election of Antibody Species
The elected species of monoclonal antibody for generic claims 1 limitation (d) VH SEQ ID NO: 25 and VL SEQ ID NO: 29; and the dependent claim 2 limitation (d) with embedded CDRs SEQ ID NO: 26-28, and SEQ ID NO: 30-32 were found free of prior art.
The search was extended for other species of the Markush election of antibody species (VH, VL, and CDRs) for compact prosecution in view of elected antibody VH and VL sequences (claim 1, 3, and 5) and CDRs sequences (claim 2) being free of prior art.
Claim 3 the VH and VL sequences recited in limitations (a) and (d) were considered from the sequence search. Sequences in limitations (b) – (c) and (e)-(o) were not considered for examination because of the claimed and required sequence prior art match found for limitation (a).
Status of Claims
3. Claims 1-29 and 32 as per claim listing filed on 02/09/2026 are pending.
4. Claims 17-23, 25-29 and 32 as per claim listing filed on 02/09/2026 are withdrawn from examination.
5. Claims 1-16, and 24 are under examination.
Priority
6. This application is a 371 of PCT/US2022/015341 and claims the benefit of U.S. provisional application no. 63/147,419, filed February 9, 2021.
Information Disclosure Statement
7. Three information disclosure statements (IDSs) submitted on 08/02/2023, 12/18/2024, 02/09/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Objection to Specification/Drawings
8. The drawings are objected to because a few drawings are not clearly legible to read and examine.
The drawings: FIG. 1A, FIG. 8, FIG. 9, FIG. 17A, Fig 17 C, Fig 18 E, FIG. 20B, FIG. 21E, FIG. 23B, FIG. 23C, FIG. 24A, FIG. 25A, FIG. 26A, and FIG. 29C.
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 renumbered 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.
In addition to Replacement Sheets containing the corrected drawing figure(s), applicant is required to submit a marked-up copy of each Replacement Sheet including annotations indicating the changes made to the previous version. The marked-up copy must be clearly labeled as “Annotated Sheets” and must be presented in the amendment or remarks section that explains the change(s) to the drawings. See 37 CFR 1.121(d)(1). Failure to timely submit the proposed drawing and marked-up copy will result in the abandonment of the application.
9. The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant’s cooperation is requested in correcting any errors of which applicant may become aware in the specification.
Claim Rejections - 35 USC § 112
10. 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 3 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 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.
According to the instant specification, the claimed isolated monoclonal antibody, or an antigen binding fragment thereof, which binds to SARS-CoV-2 spike protein and neutralizes SARS-CoV-2 virus comprises a variable heavy (VH) domain and a variable light (VL) domain comprise amino acid sequences that have an overall 90% sequence identity to the VH and VL domains of a monoclonal antibody derived from B cell of SARS CoV-2 virus infection recovered individuals, and or recovered individual. In certain embodiments the monoclonal antibody is a recombinant monoclonal antibody and is produced by a host cell into which an expression vector(s) encoding the antibody, or fragment thereof, has been transfected (Instant specification, page no. 118).
The scope of claim 3 is generic (very broad) because the claim recites a genus of a monoclonal antibody comprising 10% amino acid variation (90% amino acid identity). The claim 3 recites limitations that are generic, and the specification does not have support commensurate with the full scope of the claimed invention, “a monoclonal antibody, or an antigen binding fragment thereof, which binds to and neutralize SARS-COV-2 spike protein with at least 90% sequence identity to the VH and VL domains of an antibody or wherein the VH domain and VL domain each have at least 90% sequence identity to the VH and VL domains, respectively, is claimed by reciting specific antibody VH and VL sequences (e.g. claim 3 (d) SEQ ID NO: 25 and 29). The claim 3 allows up to 10% amino acid substitutions introducing variant species of “a claimed monoclonal antibody or antibodies”.
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 10% variation (90% identity) resulting in “variant” antibody or fragments or fragments thereof encompassed by the instant claim 3 may or may not be effective in achieving the neutralizing efficacy or binding affinities similar to the antibodies that are derived from wild type and recombinant amino acid sequences (without mutations/substitution/variations) in the claimed VH/VL (CDR sequences). Specifically in relation to antibody 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 2001, 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 1982, 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).
The instant specification does not have written description support by reduction to practice of example(s) showing that that the applicant possesses the claimed recombinant antibody variants (90% amino acid identity to the wildtype antibody VH+VL or six CDR sequences CDR H1-H3 and CDR L1-L3) that comprise 10% variation in amino acid sequence that is required to be satisfied through sufficient description of a representative number of species by actual reduction to practice showing similar binding to spike protein and neutralizing efficacy of a SARS-CoV-2 coronavirus. Many different variants of recombinant antibody or the antigen binding fragment thereof are possible and can be envisioned by the ordinary skills given 10% amino acid variation (90% identity).
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, reduction to drawings, 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 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”.
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).
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 full scope of claimed invention as claimed in claim 3 since there is no or insufficient representative species and/or identifying characteristics to place applicant in possession of the generic scope of the claimed invention directed to a recombinant antibody comprising amino acid sequence with 90% identity (comprising 10% amino acid variation) and has a function of binding to spike protein of SARS-CoV-2 virus and neutralizing of SARS-CoV-2 virus.
Claim Rejections - 35 USC § 112
11. 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.
Claim 5 is 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 instant claim 5 is directed to the isolated monoclonal antibody or antigen binding fragment of any one (reads on the claimed antibodies of claim 1) of claim 1. The subject matter of the instant claim 5 fails to further limit the scope of claim 1 on which the instant claim 5 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 Interpretation
12. 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: An isolated monoclonal antibody or antigen binding fragment thereof, comprising: a) a heavy chain variable (VH) region and a light chain variable region (VL) comprising a heavy chain complementarity determining region (HCDR)1, a HCDR2, and a HCDR3, and a light chain complementarity determining region (LCDR)1, a LCDR2, and a LCDR3 of the VH and VL set forth as SEQ ID NOs: 25 and 29, respectively (elected species SEQ ID NOs: 25 and 29), and wherein the monoclonal antibody specifically binds to a coronavirus spike protein, and neutralizes SARS-CoV-2.
The claimed monoclonal antibody is interpreted to be directed to an isolated monoclonal antibody that is recombinantly derived from a single memory B cell of obtained from a SARS CoV-2 survivor 48 days following symptom onset in an individual (See, instant specification, page 99 example 12 lines 20-21; page 116, example 22, line 6-7 PBMCs from SARS CoV-2 subjects) and thus, a monoclonal antibody is produced by the single memory B cell and the monoclonal antibody bind and neutralize SARS-CoV-2 virus (See, instant specification, page 14, lines 13-16). The monoclonal antibody is also interpreted to comprise wild type HV and VL sequence without amino acid substitution to generate a recombinant monoclonal antibody (See, instant specification, page 99 example 12 lines 20-21). An antibody in a broadest sense is interpreted as a polyclonal antibody that comprise many monoclonal antibodies that bind to spike protein and neutralize SARS-CoV-2 virus (See, instant specification, page 15, lines 25-30).
Claim Rejections - 35 USC § 101
13. 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 1-16, and 24 are rejected under 35 U.S.C. 101 because according to the broadest reasonable interpretation (BRI) in view of the instant specification, the claim 1 (and dependent claims 2-16, and 24) are interpreted to be directed to a product of nature, an isolated monoclonal antibody that is recombinantly derived from a single memory B cell of obtained from a SARS CoV-2 survivor 48 days following symptom onset in an individual (See, instant specification, page 99 example 12 lines 20-21; page 116, example 22, line 6-7 PBMCs from SARS CoV-2 subjects) and thus, a monoclonal antibody is produced by the single memory B cell and the monoclonal antibody bind and neutralize SARS-CoV-2 virus (See, instant specification, page 14, lines 13-16). The monoclonal antibody is also interpreted to comprise wild type HV and VL sequence without amino acid substitution to generate a recombinant monoclonal antibody (See, instant specification, page 99 example 12 lines 20-21). An antibody in a broadest sense is interpreted as a polyclonal antibody that comprise many monoclonal antibodies that bind to spike protein and neutralize SARS-CoV-2 virus (See, instant specification, page 15, lines 25-30).
Step 1: According to MPEP § 2106, the claimed invention must be to one of the four statutory categories. According to 35 U.S.C. 101 the eligibility test, the claim 1 (and dependent claims 2-16, and 24) are directed to a statutory category, e.g. composition of matter (the claimed monoclonal antibody with a function of binding to a SARS-CoV-2 virus spike protein and neutralization of SARS-CoV-2 virus), therefore, statutory category eligibility, Step 1: Yes.
Step 2: As described in the instant specification and the prior art Cao et al 2020, Zost et al 2020, and Liu et al 2020 recited below the claimed genus of monoclonal antibody or recombinant monoclonal antibody is produced by a human single B cell (plasma cell) in response to a SARS-CoV-2 virus infection and can be termed as a monoclonal antibody which naturally comprise the antigen binding fragment, Fc, VH and VL chains. The antibody has a function of binding to spike protein (surface protein of a coronavirus) and neutralizing a SARS-CoV-2 virus. The claimed recombinant monoclonal antibodies uses the VL and VL sequences from the B cell and does not have markedly different characteristics or function from what exist in nature or human, and thus is “a product of nature” exception, Step 2A: Prong 1- Yes :claim 1 (and dependent claims) recite a “judicial exception” a product of nature.
The claim 1 (and dependent claims 2-16, and 24) fails to integrate (e.g. composition of matter-the claimed monoclonal antibody with a function of binding to a SARS-CoV-2 virus spike protein) the judicial exception into a practical application (e.g method of treatment, diagnostic assay or purification) or contain additional elements that result in a “markedly different” antibody as compared to the natural counterpart, Step 2A: Prong 2-No.
The claim 1 (and dependent claims 2-16, and 24) does/do not include additional elements that are sufficient to amount to significantly more to the claimed composition of matter a monoclonal antibody (a genus) (than the judicial exception because the claims recite a monoclonal antibody and additional antibody species in the genus, as to constitute an “inventive concept” (e.g. improvement) Step 2B: No.
Cao et al 2020 teaches SARS CoV-2 spike RBD domain binding neutralizing and non-neutralizing monoclonal antibodies obtained from a B cell or plasma cell, by using recombinant DNA technology tools and methods, of an individual that was known to be infection with SARS-CoV-2 virus (See, abstract, entire article).
Zost et al 2020 teaches potent neutralizing mAbs recognizing non-overlapping sites, COV2-2196 and COV2-2130 (RBD binding or ACE2 blocking), bound simultaneously to Spike protein and synergistically neutralized authentic SARS-CoV-2 virus. A large panel of SARS-CoV-2 Spike protein-reactive mAbs from the B cells of two convalescing individuals who had been infected with SARS-CoV-2 in Wuhan China. The antibodies were isolated using diverse tools for isolation and cloning of single antigen-specific B cells and the antibody variable genes encoding monoclonal antibodies. The Mabs were potently neutralizing and protective human antibodies against SARS-CoV-2. The Mabs were specific for RBD, S2 and ACE2 blocking neutralizing function (See, abstract, Figure 1-2, section on Antibodies, entire article).
Liu et al 2020 teaches potent neutralizing monoclonal antibodies (recombinantly obtained using recombinant DNA technology and methods) against multiple epitopes on SARS-CoV-2 spike protein. Isolation of sixty-one SARS-CoV-2-neutralizing monoclonal antibodies from B cells of five patients infected with SARS-CoV-2 and admitted to hospital with severe coronavirus disease 2019 (COVID-19). Among these are nineteen antibodies that potently neutralized authentic SARS-CoV-2 in vitro, nine of which exhibited very high potency, with 50% virus-inhibitory concentrations of 0.7 to 9 ng ml−1. Epitope mapping showed that this collection of nineteen antibodies was about equally divided between those directed against the receptor-binding domain (RBD) and those directed against the N-terminal domain (NTD), indicating that both of these regions at the top of the viral spike are immunogenic. In addition, two other powerful neutralizing antibodies recognized quaternary epitopes that overlap with the domains at the top of the spike. Cryo-electron microscopy reconstructions of one antibody that targets the RBD, a second that targets the NTD, and a third that bridges two separate RBDs showed that the antibodies recognize the closed, ‘all RBD-down’ conformation of the spike. Several of these monoclonal antibodies are promising candidates for clinical development as potential therapeutic and/or prophylactic agents against SARS-CoV-2 (See, abstract, Fig 1-4, page 451 col 1 section on Isolation and construction of mAbs).
Tortorici et al 2020 teaches neutralization of SARS-CoV-2 by isolated monoclonal antibody S2E12 and S2M11 IgG or Fab by binding to RBD of spike protein. Peripheral blood samples were obtained from two donors who have recovered from SARS-CoV-2 infection. Samples were collected 46 and 61 days after symptoms onset, respectively. (See, Fig. 1, methods, entire article).
Thus, the claim 1 (and dependent claims 2-16, and 24) are rejected under 35 U.S.C. 101 as the claimed monoclonal antibody is a product of nature without modification of the sequence and the claims are directed to a genus of monoclonal antibody that encompass entire B cell repertoire of VH and VL chain sequence comprising monoclonal antibodies from a SARS-CoV-2 infected individual’s B cell or plasma cells as recited supra, and because the claim does not include any additional features that could add significantly more to the exception.
Claim Rejections - 35 USC § 103
14. 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.
Claims 1-16 and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Babb et al 2020 (US10787501B1, 09/29/2020), and further in view of Lanzavecchia et al 2012 (US8124093B2, published 02/28/2012), Ahmed et al 2016 (US9469685B2, published 10/18/2016), Campbell et al 2011 (US7910708B2, published 03/22/2011), Papadopoulos et al 2011 (US7919593B2, published 04/05/2011), Stevens et al 2009 (US7582298B2, published 09/01/2009), Nioi et al 2019 (US10358497B2, published 07/23/2019), Smider et al 2015 (US9221902B2, published 12/29/2012), Haber et al 2020 (US10738130B2, 08/11/2020),
Cao et al 2020 (Cell. 2020 Jul 9;182(1):73-84.e16.), Zost et al 2020 (Nature. 2020 Aug;584(7821):443-449), Liu et al 2020 (Nature. 2020 Aug;584(7821):450-456. doi: 10.1038/s41586-020-2571-7), and Tortorici et al 2020 (Science. 2020 Nov 20;370(6519):950-957), Pinto et al 2020 (Nature. 2020 Jul;583(7815):290-295), and Hinton et al 2004 (J Biol Chem. 2004 Feb 20;279(8):6213-6).
Claims 1-16 and 24: Babb et al 2020 (US10787501B1) teaches an isolated monoclonal antibody or antigen-binding fragment thereof that binds a SARS-CoV-2 spike protein and neutralize SARS-CoV-2, however, does not teach the claimed VH, VL, six CDR sequences in instant claim 1 isolated monoclonal antibody claimed in limitation (o) SEQ ID NO: 143 and 5; instant claim 2 isolated monoclonal antibody CDR sequences claimed in limitation (o) the HCDR1, the HCDR2, the HCDR3, the LCDR1, the LCDR2, and the LCDR3 comprise the amino acids sequences set forth as SEQ ID NOs: 2, 3, 58, 6, 7, 8, respectively; instant claim 3 isolated monoclonal antibody VH and VL sequence with 90% identity claimed in limitation (o) SEQ ID NO: 143 and 5; instant claim 5 isolated monoclonal antibody VH and VL sequence claimed in limitation (o) SEQ ID NO: 143 and 5, respectively.
The prior arts as recited below teaches six CDRs amino acid sequences SEQ ID NO: 2, 3, 58, 6, 7, and 8 of instant claim 2.
Lanzavecchia et al 2012 (US8124093B2, published 02/28/2012) disclosed SEQ ID NO: 232 (Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 2, as recited below.
Query Match 100.0%; Score 40; Length 8;
Best Local Similarity 100.0%;
Matches 8; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GFTFTSSA 8
||||||||
Db 1 GFTFTSSA 8
Ahmed et al 2016 (US9469685B2, published 10/18/2016) disclosed SEQ ID NO: 8661 (Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 3, as recited below.
Query Match 100.0%; Score 39; Length 8;
Best Local Similarity 100.0%;
Matches 8; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 IVVGSGNT 8
||||||||
Db 1 IVVGSGNT 8
Campbell et al 2011 (US7910708B2, published 03/22/2011) disclosed SEQ ID NO: 1 (Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 58, as recited below.
Query Match 100.0%; Score 46; Length 8;
Best Local Similarity 100.0%;
Matches 8; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GFTFSNYG 8
||||||||
Db 1 GFTFSNYG 8
Papadopoulos et al 2011 (US7919593B2, published 04/05/2011) disclosed SEQ ID NO: 142 (Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 6, as recited below.
Query Match 100.0%; Score 32; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QSVSSSY 7
|||||||
Db 1 QSVSSSY 7
Stevens et al 2009 (US7582298B2, published 09/01/2009) disclosed SEQ ID NO: 15 (Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 7, as recited below.
Query Match 100.0%; Score 14; Length 3;
Best Local Similarity 100.0%;
Matches 3; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GAS 3
|||
Db 1 GAS 3
Nioi et al 2019 (US10358497B2, published 07/23/2019) disclosed SEQ ID NO: 26764
(Db) that has 100% sequence identity with instant claim 2 SEQ ID NO: 8, as recited below.
Query Match 100.0%; Score 71; Length 108;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 CQQYGNSPWTF 11
|||||||||||
Db 89 CQQYGNSPWTF 99
Cao et al 2020 teaches SARS CoV-2 spike RBD domain binding neutralizing and non-neutralizing monoclonal antibodies obtained from a B cell or plasma cell, by using recombinant DNA technology tools and methods, of an individual that was known to be infection with SARS-CoV-2 virus (See, abstract, entire article).
Zost et al 2020 teaches potent neutralizing mAbs recognizing non-overlapping sites, COV2-2196 and COV2-2130 (RBD binding or ACE2 blocking), bound simultaneously to Spike protein and synergistically neutralized authentic SARS-CoV-2 virus. A large panel of SARS-CoV-2 Spike protein-reactive mAbs from the B cells of two convalescing individuals who had been infected with SARS-CoV-2 in Wuhan China. The antibodies were isolated using diverse tools for isolation and cloning of single antigen-specific B cells and the antibody variable genes encoding monoclonal antibodies. The Mabs were potently neutralizing and protective human antibodies against SARS-CoV-2. The Mabs were specific for RBD, S2 and ACE2 blocking neutralizing function (See, abstract, Figure 1-2, section on Antibodies, entire article).
Liu et al 2020 teaches potent neutralizing monoclonal antibodies (recombinantly obtained using recombinant DNA technology and methods) against multiple epitopes on SARS-CoV-2 spike protein. Isolation of sixty-one SARS-CoV-2-neutralizing monoclonal antibodies from B cells of five patients infected with SARS-CoV-2 and admitted to hospital with severe coronavirus disease 2019 (COVID-19). Among these are nineteen antibodies that potently neutralized authentic SARS-CoV-2 in vitro, nine of which exhibited very high potency, with 50% virus-inhibitory concentrations of 0.7 to 9 ng ml−1. Epitope mapping showed that this collection of nineteen antibodies was about equally divided between those directed against the receptor-binding domain (RBD) and those directed against the N-terminal domain (NTD), indicating that both of these regions at the top of the viral spike are immunogenic. In addition, two other powerful neutralizing antibodies recognized quaternary epitopes that overlap with the domains at the top of the spike. Cryo-electron microscopy reconstructions of one antibody that targets the RBD, a second that targets the NTD, and a third that bridges two separate RBDs showed that the antibodies recognize the closed, ‘all RBD-down’ conformation of the spike. Several of these monoclonal antibodies are promising candidates for clinical development as potential therapeutic and/or prophylactic agents against SARS-CoV-2 (See, abstract, Fig 1-4, page 451 col 1 section on Isolation and construction of mAbs).
Tortorici et al 2020 teaches neutralization of SARS-CoV-2 by isolated monoclonal antibody S2E12 and S2M11 IgG or Fab by binding to RBD of spike protein. Peripheral blood samples were obtained from two donors who have recovered from SARS-CoV-2 infection. Samples were collected 46 and 61 days after symptoms onset, respectively. (See, Fig. 1, methods, entire article).
It would have been obvious to combine the prior art teachings as recited supra on the six CDR sequences disclosed individually by Lanzavecchia et al 2012, Ahmed et al 2016, Campbell et al 2011, Papadopoulos et al 2011, Stevens et al 2009, and Nioi et al 2019 to construct the VH and VL sequences SEQ ID NO: 143 and SEQ ID NO: 5 as claimed in instant claims 1, 3, and 5 claim limitation (o) and CDR sequences as claimed in instant claim 2 limitation (o) to produce the claimed antibody by recombinant molecular biology technique known in the art for production of monoclonal antibodies that bind to spike protein and neutralize SARS-CoV-2, and the method and techniques taught by Babb et al 2020, Cao et al 2020, Zost et al 2020, Liu et al 2020, and Tortorici et al 2020 (See, entire prior arts) to produce and arrive at the invention of the claimed monoclonal antibody that has a function of binding to spike protein and neutralize SARS-CoV-2.
Claim 3: The combined teachings of Smider et al 2015 and Haber et al 2020 teaches added limitation of instant claim 3 (a) as recited below by disclosing the VH SEQ ID NO: 1 and VL SEQ ID NO: 5 sequence that has at least 90% identical amino acid sequence.
Smider et al 2015 (US9221902B2, published 12/29/2012) disclosed SEQ ID NO: 1516 that has 90.8% identity with instant claim 3 SEQ ID NO: 1 as recited below.
Query Match 90.8%; Score 590.5; Length 126;
Best Local Similarity 91.3%;
Matches 115; Conservative 5; Mismatches 3; Indels 3; Gaps 2;
Qy 1 QMQLVQSGPEVKKPGTSVKVSCKASGFTFTSSAVQWVRQARGQRLEWIGWIVVGSGNTNY 60
|||||||||||||||||||||||||||||||||:||||||||||||||||||||||||||
Db 1 QMQLVQSGPEVKKPGTSVKVSCKASGFTFTSSAMQWVRQARGQRLEWIGWIVVGSGNTNY 60
Qy 61 AQKFQERVTITRDMSTSTAYMELSSLRSEDTAVYYCAAP-YCSGGSCFD--GFDIWGQGT 117
|||||||||||||||||||||||||||||||||||||| |||||||: ||:||:||
Db 61 AQKFQERVTITRDMSTSTAYMELSSLRSEDTAVYYCAAEGYCSGGSCYSYWYFDLWGRGT 120
Qy 118 MVTVSS 123
:|||||
Db 121 LVTVSS 126
Haber et al 2020 (US10738130B2, 08/11/2020) disclosed SEQ ID NO: 338 that has 98.4% identity with instant claim 3 SEQ ID NO: 5 as recited below.
Query Match 98.4%; Score 557; Length 108;
Best Local Similarity 98.1%;
Matches 106; Conservative 1; Mismatches 1; Indels 0; Gaps 0;
Qy 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGFP 60
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||| |
Db 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIP 60
Qy 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGNSPWTFGQGTKVEIR 108
|||||||||||||||||||||||||||||||||||||||||||||||:
Db 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGNSPWTFGQGTKVEIK 108
It would have been obvious to combine the prior art teachings of Smider et al 2015 and Haber et al 2020 to produce the monoclonal antibody and arrive at the invention of the claimed monoclonal antibody that has a function of binding to spike protein and neutralize SARS-CoV-2.
Claim 4: Babb et al 2020 the added limitation a human framework region and teaches anti-SARS-CoV-2 mAbs derived from human (See, Description col 11 para 1, col 12 para 1).
Claim 6: Babb et al 2020 the added limitation antibody comprises a human constant domain and also teaches anti-SARS-CoV-2 mAbs derived from human (See Description).
Claim 7: Babb et al 2020 that teaches the added limitation isolated monoclonal antibody is a human antibody by disclosing anti-SARS-CoV-2 mAbs derived from human (See Description).
Claim 8: Babb et al 2020 the added limitation isolated monoclonal antibody is an IgA and also teaches anti-SARS-CoV-2 mAbs derived from human (See, Description, col 12 para 3).
Claim 9: Babb et al 2020 the added limitation a recombinant constant domain comprising a modification that increases the half-life of the antibody (See, Description, Col 40, para 4-5).
Claim 10: Hinton et al 2004 teaches the added limitation, wherein the modification increases binding to the neonatal Fc receptor. Hinton et al 2004 teaches the neonatal Fc receptor (FcRn) plays an important role in regulating the serum half-lives of IgG antibodies. Following mutagenesis, several IgG2 mutants with increased binding affinity to human FcRn at pH 6.0 were identified at Fc positions 250 and 428. A pharmacokinetics study of two mutant IgG2 antibodies with increased FcRn binding affinity indicated that they had serum half-lives in rhesus monkeys approximately 2-fold longer than the wild-type antibody. (See, abstract, entire article). The teachings of Hinton et al 2004 are applicable and renders obvious the added limitation of instant claim 10.
Claim 11: The combined prior art teachings as applied to the claim 1 above teaches the VH and VL sequence of the isolated monoclonal antibody. Therefore, combined prior art teachings as applied to claim 1 as recited supra teaches the added limitation, wherein the antibody specifically binds an N-terminal domain of the coronavirus spike protein. In addition, Cao et al 2020 teaches the S1 subunit at the N-terminal region is responsible for virus attachment and contains the receptor-binding domain (RBD), which directly binds to the ACE2 receptor on the host cell. Cao et al 2020, Zost et al 2020, and Tortorici et al 2020 teaches ACE-2 receptor binding monoclonal antibody (See, abstract, introduction, entire article).
Claim 12: Babb et al 2020 teaches the added limitation, wherein the antibody specifically binds a receptor binding domain (RBD) of the coronavirus spike protein (See, legends for Fig 11-13, description).
Claim 13: The combined prior art teachings as applied to the claim 1 above teaches the VH and VL sequence of the isolated monoclonal antibody. Therefore, combined prior art teachings as applied to claim 1 as recited supra teaches the added limitation, wherein the antibody neutralizes SARS-CoV-1. In addition, Pinto et al 2020 teaches cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV (reads on SARS-CoV-1) antibody.
Claim 14: Babb et al 2020 teaches the added limitation, the antigen binding fragment of claim 1 (See, claim 1, abstract, description).
Claim 15: Babb et al 2020 teaches the added limitation, wherein the antigen binding fragment is a Fv, Fab, F(ab')2, scFV or a scFV2 fragment (See, claim 1, abstract, description).
Claim 16: Babb et al 2020 teaches the added limitation 1, conjugated to a detectable marker (See, Babb et al 2020, US10787501B1, col 53 para 1).
Claim 24: Babb et al 2020 teaches a pharmaceutical, comprising an effective amount of the monoclonal antibody or the antigen binding fragment of claim 1, a bispecific antibody comprising the monoclonal antibody or antigen binding fragment, a nucleic acid molecule encoding the monoclonal antibody, antigen binding fragment or bispecific antibody, or a vector comprising the nucleic acid molecule; and a pharmaceutically acceptable carrier (See, Babb et al 2020, US10787501B1, claims 13-20, abstract, Description).
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 Babb et al 2020 with additional teachings of Lanzavecchia et al 2012, Ahmed et al 2016, Campbell et al 2011, Papadopoulos et al 2011, Stevens et al 2009, Nioi et al 2019 on the six CDR sequences or Smider et al 2015, and Haber et al 2020 on at least 90% identity VH and VL sequences SEQ ID NOs: 1 and 5 (claim 3) of the claimed isolated monoclonal antibody and combine the CDR sequences to construct and produce the monoclonal antibody with additional teachings on the added dependent claim limitations of Babb et al 2020, Cao et al 2020, Zost et al 2020, Liu et al 2020, Tortorici et al 2020, and Pinto et al 2020, and Hinton et al 2004 to arrive at the inventions of claims 1-16 and 24 as recited supra. One of the ordinary skills in the art would have been motivated to develop strong spike protein binding monoclonal antibody against SARS-CoV-2 for developing immunodiagnostics assays and kits; and for developing potent SARS-CoV-2 neutralizing monoclonal antibody with longer half-life and stability for therapeutics for commercial success. There would have been a reasonable expectation of success given the applied prior arts teachings and required research 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 1-16 and 24. 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).
Double Patenting
15. The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
16. Claims 1-16 and 24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10, and 15-30 of copending Application No. 19/141,012 in view of combined teachings of Babb et al 2020 (US10787501B1, 09/29/2020), Lanzavecchia et al 2012 (US8124093B2, published 02/28/2012), Ahmed et al 2016 (US9469685B2, published 10/18/2016), Campbell et al 2011 (US7910708B2, published 03/22/2011), Papadopoulos et al 2011 (US7919593B2, published 04/05/2011), Stevens et al 2009 (US7582298B2, published 09/01/2009), Nioi et al 2019 (US10358497B2, published 07/23/2019), Smider et al 2015 (US9221902B2, published 12/29/2012), Haber et al 2020 (US10738130B2, 08/11/2020), Cao et al 2020 (Cell. 2020 Jul 9;182(1):73-84.e16.), Zost et al 2020 (Nature. 2020 Aug;584(7821):443-449), Liu et al 2020 (Nature. 2020 Aug;584(7821):450-456. doi: 10.1038/s41586-020-2571-7), and Tortorici et al 2020 (Science. 2020 Nov 20;370(6519):950-957), Pinto et al 2020 (Nature. 2020 Jul;583(7815):290-295), and Hinton et al 2004 (J Biol Chem. 2004 Feb 20;279(8):6213-6).
The instant claims 1-16 and 24 and the copending claims 1-10, and 15-30 are directed to an isolated monoclonal antibody or antigen binding fragment thereof, wherein the monoclonal antibody specifically binds to a coronavirus spike protein and neutralizes SARS-CoV-2.
The instant claims and the copending claims may differ in structure of the antibody CDRs, however, the applicant has claimed a genus of the isolated monoclonal antibodies, and both the instant and co-pending monoclonal antibodies are isolated from B cells of SARS-CoV-2 infected individuals that comprise a broad repertoire of anti- SARS-CoV-2 spike protein binding and neutralizing antibodies and the combined teachings of prior arts as recited supra under 35 U.S.C 103 rejection renders obvious the obvious modification of the copending claims as variant of instant claims for motivation of developing a anti-SARS-CoV-2 therapy and immunoassay diagnostics methods with a reasonable expectation of success within the skills of the ordinary rendering the copending variant claims obvious.
This is a provisional nonstatutory double patenting rejection.
17. Claims 1-16 and 24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of copending Application No. 19/109,315 in view of combined teachings of Babb et al 2020 (US10787501B1, 09/29/2020), Lanzavecchia et al 2012 (US8124093B2, published 02/28/2012), Ahmed et al 2016 (US9469685B2, published 10/18/2016), Campbell et al 2011 (US7910708B2, published 03/22/2011), Papadopoulos et al 2011 (US7919593B2, published 04/05/2011), Stevens et al 2009 (US7582298B2, published 09/01/2009), Nioi et al 2019 (US10358497B2, published 07/23/2019), Smider et al 2015 (US9221902B2, published 12/29/2012), Haber et al 2020 (US10738130B2, 08/11/2020),
Cao et al 2020 (Cell. 2020 Jul 9;182(1):73-84.e16.), Zost et al 2020 (Nature. 2020 Aug;584(7821):443-449), Liu et al 2020 (Nature. 2020 Aug;584(7821):450-456. doi: 10.1038/s41586-020-2571-7), and Tortorici et al 2020 (Science. 2020 Nov 20;370(6519):950-957), Pinto et al 2020 (Nature. 2020 Jul;583(7815):290-295), and Hinton et al 2004 (J Biol Chem. 2004 Feb 20;279(8):6213-6).
The instant claims 1-29 and 32 and the copending claims 1-30 are directed to an isolated monoclonal antibody or antigen binding fragment thereof, wherein the monoclonal antibody specifically binds to a coronavirus spike protein and neutralizes SARS-CoV-2.
The instant claim 3 SEQ ID NO: 1 and SEQ ID NO: 5 has >90% identity with the copending claim 3 monoclonal antibody as recited below.
SEQ ID NO: 1 (Qy= instant claims) with SEQ ID NO: 1 (Db = copending claims).
Query Match 100.0%; Score 650; DB 1; Length 123;
Best Local Similarity 100.0%;
Matches 123; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QMQLVQSGPEVKKPGTSVKVSCKASGFTFTSSAVQWVRQARGQRLEWIGWIVVGSGNTNY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QMQLVQSGPEVKKPGTSVKVSCKASGFTFTSSAVQWVRQARGQRLEWIGWIVVGSGNTNY 60
Qy 61 AQKFQERVTITRDMSTSTAYMELSSLRSEDTAVYYCAAPYCSGGSCFDGFDIWGQGTMVT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AQKFQERVTITRDMSTSTAYMELSSLRSEDTAVYYCAAPYCSGGSCFDGFDIWGQGTMVT 120
Qy 121 VSS 123
|||
Db 121 VSS 123
SEQ ID NO: 5 (Qy= instant claims) with SEQ ID NO: 5 (Db = copending claims).
Query Match 95.0%; Score 537.5; DB 1; Length 109;
Best Local Similarity 96.3%;
Matches 105; Conservative 1; Mismatches 2; Indels 1; Gaps 1;
Qy 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGFP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGFP 60
Qy 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGN-SPWTFGQGTKVEIR 108
||||||||||||||||||||||||||||||||| : ||||||||||||
Db 61 DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGGLTGWTFGQGTKVEIR 109
The instant claims and the copending claims may differ in structure of the antibody CDRs, however, the applicant has claimed a genus of the isolated monoclonal antibodies, and both the instant and co-pending monoclonal antibodies are isolated from B cells of SARS-CoV-2 infected individuals that comprise a broad repertoire of anti- SARS-CoV-2 spike protein binding and neutralizing antibodies and the combined teachings of prior arts as recited supra under 35 U.S.C 103 rejection renders obvious the obvious modification of the copending claims as variant of instant claims for motivation of developing anti-SARS-CoV-2 therapy and immunoassay diagnostics methods with a reasonable expectation of success within the skills of the ordinary rendering the copending variant claims obvious.
This is a provisional nonstatutory double patenting rejection.
18. Relevant Prior Arts:
Wang et al 2021. Antibody resistance of SARS-CoV-2 variants B. 1.351 and B.1.1.7, NATURE, NATURE PUBLISHING GROUP UK, LONDON, vol. 593, no. 7857, 8 March 2021 (2021-03-08), pages 130-135, XP037443288.
Lu et al 2011. A neonatal Fc receptor-targeted mucosal vaccine strategy effectively induces HIV-1 antigen-specific immunity to genital infection. J Virol. 2011 Oct;85(20):10542-53.
Lu et al disclosed that given the role of neonatal Fc receptor (FcRn) in transferring IgG across polarized epithelial cells which line mucosal surfaces, FcRn might be useful for delivering HIV vaccine antigens (the inventive concept is applicable for mAb therapy for SARS-COV-2 mucosal infection) across mucosal epithelial barriers to the underlying antigen-presenting cells. Chimeric proteins composed of HIV Gag (p24) fused to the Fc region of IgG (Gag-Fc) bind efficiently to airway mucosa and are transported across this epithelial surface. Mice immunized intranasally with Gag-Fc plus CpG adjuvant developed local and systemic immunity, including durable B and T cell memory. Gag-specific immunity was sufficiently potent to protect against an intravaginal challenge with recombinant vaccinia virus expressing the HIV Gag protein. Intranasal administration of a Gag-Fc/CpG vaccine protected at a distal mucosal site. Targeting of FcRn with chimeric immunogens may be an important strategy for mucosal immunization and vaccines.
Conclusion
19. No claim is allowed.
20. Any inquiry concerning this communication or earlier communications from the examiner should be directed to SAMADHAN J JADHAO whose telephone number is (703)756-1223. The examiner can normally be reached M-F 8:00-5:00.
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/SAMADHAN JAISING JADHAO/ Examiner, Art Unit 1672
/BENNETT M CELSA/ Primary Examiner, Art Unit 1600
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