DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election Restrictions
Applicant’s election with traverse of Group I, claims 1-9 drawn to an immunoassay method for assaying SARS-CoV-2, in the reply filed on 04/27/2026 is acknowledged. Additionally, Applicant's election of following species:
SEQ ID NOs: 1 in claim 2
A monoclonal antibody or antibody fragment thereof of (1) in claim 9
in the reply filed on 04/27/2026 is acknowledged.
The traversal is on the ground(s) that: the shared feature among the independent claims 1, 10, and 18 was not disclosed or suggested by the cited reference, and thus it constitutes a "special technical feature" under 37 CFR 1.475, is not persuasive because the claims recite “wherein the monoclonal antibody or the antibody fragment thereof binds to SARS-CoV-2 treated with a serine protease”. This limitation as written and submitted on 11/09/2023 is unclear, because it is not clear if treatment of serine protease is performed to the entire biological sample, the monoclonal antibody or the antibody fragment thereof, the SARS-CoV-2 present in the sample, or the nucleocapsid protein of SARS-CoV-2. Further, it is unclear whether a monoclonal antibody or the antibody fragment thereof with specificity for a nucleocapsid protein of SARS-CoV-2 would be capable of binding to a nucleocapsid protein in the sample treated with a serine protease because the epitope could be cleaved thereby abolishing recognition by the monoclonal antibody or the antibody fragment thereof with specificity for a nucleocapsid protein of SARS-CoV-2. Therefore, claim 1 as submitted on 11/09/2023 is unclear. Accordingly, the common technical feature is a coronavirus antibody that binds to the nucleocapsid protein of SARS-CoV-2. Therefore, as indicated in the restriction action more completely, the technical feature of claim 1 that provides unity of invention among all claims is not a special technical feature as defined by PCT Rule 13.2 because it does not define a contribution over the prior art. Accordingly, the requirement is still deemed proper and is therefore made FINAL.
Claims 10-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Invention, there being no allowable generic or linking claim.
Claims 1-9 are under examination on the merits.
Priority
Applicant’s claim for foreign priority of prior-filed Japanese application No. 2021-100117 filed on 06/16/2021 under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Receipt is acknowledged of certified copies of documents required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) was submitted on 01/11/2024 and 11/28/2025. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawings
The drawings were received on 11/09/2023. The drawings are objected to because nucleotide and/or amino acid sequences appearing in the drawings (Figs. 1-2) are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings.
Any structural detail that is essential for a proper understanding of the disclosed invention should be shown in the drawing. MPEP § 608.02(d). 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.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/patents-application- process/filing-online/legal-framework-efs-web), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the drawings (Figs. 1-2) are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings.
Required response – Applicant must provide:
Replacement and annotated drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers;
AND/OR
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers into the Brief Description of the Drawings, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-9 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 as submitted on 04/27/2026 recites “contacting a biological sample with a monoclonal antibody or an antibody fragment thereof that binds to a nucleocapsid protein of SARS-CoV-2, wherein the monoclonal antibody or the antibody fragment thereof binds to a peptide fragment produced by treating the SARS-CoV-2 with a serine protease”. It is not clear if treatment of serine protease is performed to the entire biological sample, the SARS-CoV-2 present in the sample, or the nucleocapsid protein of SARS-CoV-2. Further, the claim requires a monoclonal antibody or the antibody fragment thereof with specificity for a nucleocapsid protein of SARS-CoV-2 and treatment of the SARS-CoV-2 with a serine protease. It is not clear if these two limitations can be satisfied because the term “a serine protease” reads on a wide genus of proteases comprising many species that could cleave the binding site of the monoclonal antibody or the antibody fragment thereof thereby abolishing binding to a nucleocapsid protein of SARS-CoV-2 (see also rejections under 35 USC § 112(a) below). The dependent claims do not provide additional clarity. Therefore, the claims are indefinite. For purposes of compact prosecution and applying prior art, claim 1 was interpreted herein as referring to the contacting a biological sample with a monoclonal antibody or an antibody fragment thereof that binds to a nucleocapsid protein of SARS-CoV-2, wherein the monoclonal antibody or the antibody fragment thereof binds to a peptide fragment produced by treating the entire biological sample, the SARS-CoV-2 present in the sample, or the nucleocapsid protein of SARS-CoV-2 with a serine protease”.
On claim 2 the recitation of “recognizes an epitope in an amino acid sequence represented by KQQTVTLLPAADLDDFSK (SEQ ID NO: 1)” should recite “recognizes an epitope in the amino acid sequence represented by KQQTVTLLPAADLDDFSK (SEQ ID NO: 1)”. For purposes of compact prosecution and applying prior art, claim 2 was interpreted herein as reciting “recognizes an epitope in the amino acid sequence represented by KQQTVTLLPAADLDDFSK (SEQ ID NO: 1)”.
On claim 5 the recitation of “wherein the monoclonal antibody or the antibody fragment comprises two types of monoclonal antibodies or antibody fragments thereof” is unclear because claim 1 requires “a monoclonal antibody or an antibody fragment thereof” which clearly indicates a single monoclonal antibody or a single antibody fragment thereof. It is not clear how a single monoclonal antibody or a single antibody fragment thereof can comprise two types of monoclonal antibodies or antibody fragments thereof as recited in claim 5. The dependent claims do not provide additional clarity. Therefore, the claims are indefinite. For purposes of compact prosecution and applying prior art, claim 5 was interpreted herein as referring to the method of claim 1 further comprising a second monoclonal antibody or a single antibody fragment thereof, wherein the second monoclonal antibody or a single antibody fragment thereof is directly or indirectly labeled and it recognizes a different epitope than that of claim 1. This affects dependent claims 6 and 7.
On claim 7 the recitation of “wherein the first monoclonal antibody or the antibody fragment thereof is a monoclonal antibody or an antibody fragment thereof that recognizes an epitope in the amino acid sequence represented by KQQTVTLLPAADLDDFSK (SEQ ID NO: 1), and the second monoclonal antibody or the antibody fragment thereof is a monoclonal antibody or an antibody fragment thereof that recognizes an epitope in the amino acid sequence represented by AADLDDFSKQLQ (SEQ ID NO: 2)” is unclear because of the following. The epitope recited in SEQ ID NO: 2 lies almost entirely within the epitope recited in SEQ ID NO: 1, with the exception of the last three amino acid residues “QLQ”. Given that the sequence in SEQ ID NO: 2 (AADLDDFSKQLQ ) is inherently present where the sequence in SEQ ID NO: 1 (KQQTVTLLPAADLDDFSK) is present within a sample and vice versa, a monoclonal antibody or an antibody fragment thereof with specificity for the epitope in SEQ ID NO: 1 would inherently recognize the epitope in SEQ ID NO: 2 and vice versa. However, claim 5, which claim 7 depends on, requires that the antibodies recognize different epitopes. It is unclear if the two antibodies required by claim 7 are considered to recognize two different epitopes, given the high sequence identity between the epitopes recited in SEQ ID NOs: 1 and 2. Further, it is unclear how these two antibodies or antibody fragments thereof could be used in an immunochromatography or ELISA assay method comprising two antibodies or antibody fragments thereof because they bind the exact same region of the N protein, and once a first complex is formed upon binding of the sample with a first antibody, the second antibody would not be able to bind that very same region. For purposes of compact prosecution and applying prior art, claim 7 was interpreted herein as referring to the method of claim 5 comprising a monoclonal antibody or an antibody fragment thereof that recognizes an epitope in the amino acid sequence comprising SEQ ID NO: 1, or a monoclonal antibody or antibody fragment thereof that recognizes an epitope in the amino acid sequence comprising SEQ ID NO: 2.
It is noted that any interpretation of the claims set forth above does not relieve Applicant of the responsibility of responding to this Office Action. If the actual interpretation of the claims is different than that posited by the Examiner, additional rejections and art may be readily applied in a subsequent final Office Action.
Claim Rejections - 35 USC § 112 - Written Description
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 1-8 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.
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, e.g., Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010); University of California v. Eli Lilly & Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) at 1406; Juno Therapeutics, Inc. v. Kite Pharma, Inc., 10 F.4th 1330, 1337, 2021 USPQ2d 893 (Fed. Cir. 2021) ("[T]he written description must lead a person of ordinary skill in the art to understand that the inventor possessed the entire scope of the claimed invention. Ariad, 598 F.3d at 1353–54 ('[T]he purpose of the written description requirement is to ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor's contribution to the field of art as described in the patent specification.' (internal quotation marks omitted).").
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.”
The instant claims are directed to a method that requires a monoclonal antibody or antigen-binding fragment thereof with the ability to bind the nucleocapsid protein of SARS-CoV-2 at the epitope as recited in instant SEQ ID NO: 28. As such the instant claims comprise a monoclonal antibody wherein sequence truncations to generate fragments thereof can be made anywhere in the antibody amino acid sequence including the heavy chain variable region and the light chain variable region including within the CDRs. Such fragments are also required to have the ability to bind the nucleocapsid protein of SARS-CoV-2 at the epitope as recited in instant SEQ ID NO: 28.
However, while the claims are drawn to a genus that comprises innumerable sequences, the Specification has only adequately described and successfully reduced to practice the full-length antibodies (Specification pages 47-63). This is not representative of the extremely large genus of sequences claimed, since no fragments, of the recited antibodies are demonstrated to have the ability to bind the nucleocapsid protein of SARS-CoV-2 at the epitope as recited in instant SEQ ID NO: 28.
It is known in the art that even the most minor differences can have significant effects on antigen-antibody binding ability; see Rudikoff et al. (cited in Applicant’s IDS submitted on 11/28/2025). The art relating to antibodies recognizes that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs 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 that is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. Further, as Rudikoff et al. teach, alterations of a single amino acid in the CDR regions of a phosphocholine-binding myeloma antibody or antigen-binding fragment thereof resulted in the loss of antigen-binding function.
Further, the instant claimed method requires treatment of the sample with a serine protease. Human serine proteases alone comprise a wide family of proteases (about 180 members) with variations as nucleoporin, lactoferrin, type II transmembrane family serine proteases (TTSP), etc. See Patel 2017 (Patel, S. “A critical review on serine protease: Key immune manipulator and pathology mediator.” Allergologia et immunopathologia vol. 45,6 (2017): 579-591. See 892-Notice of References Cited). Serine proteases have substrate specificity wherein the target of each serine protease seems to be different. The enzymes are divided into many clans/superfamilies (further divided into families), based on catalytic site topology and further their target sequence (Patel, page 2). The instant claims read on treatment of the sample with any serine protease, however, the Specification has only adequately described and successfully reduced to practice treatment of the sample with trypsin (Specification pages 47-63). This is not representative of the extremely large genus of serine proteases as claimed, since no other serine protease was shown to adequately treat the sample to generate a peptide fragment as recited in SEQ ID NO: 28.
Therefore, in light of the knowledge in the art, the broad scope of the claims, and the teachings in the Specification, it is asserted that there is still a high level of uncertainty as to which antibody fragments and which serine proteases fall within the scope of the indicated genera while retaining the ability to bind the nucleocapsid protein of SARS-CoV-2 at the epitope as recited in instant SEQ ID NO: 28, and the ability to adequately treat the sample to generate a peptide fragment as recited in SEQ ID NO: 28, respectively.
In the absence of a representative number of examples, the Specification must at least describe the structural features that are required for the claimed function. However, as discussed above, the Specification fails to describe any substantive structural limitations as to establish a structure-function relationship with respect to binding of the nucleocapsid protein of SARS-CoV-2 at the epitope as recited in instant SEQ ID NO: 28, and the ability to adequately treat the sample to generate a peptide fragment as recited in SEQ ID NO: 28.
Thus, in view of the reasons set forth above, the claims as currently written are not adequately described and one of skill in the art would readily appreciate that Applicant was not in possession of the claimed genus at the time of filing.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-8 are rejected under 35 U.S.C. 103 as being unpatentable over Tian, Xingui et al. “Epitope mapping of severe acute respiratory syndrome-related coronavirus nucleocapsid protein with a rabbit monoclonal antibody.” Virus research vol. 300 (2021): 198445, cited in Applicant’s IDS submitted on 01/11/204, in view of US PGPub 2022/0074938 A1 to Omir et al. filed on 05/07/2021, see PTO-892: Notice of References Cited.
See claims as submitted on 04/27/2026
Regarding claim 1, Tian et al. teach an immunoassay method comprising an Indirect enzyme-linked immunosorbent assay (ELISA) for detection of SARS-CoV-2 in a sample comprising contacting the sample with a SARS-CoV-2 antibody specific for the nucleocapsid protein of SARS-CoV-2, wherein the antibody binds to a region of the C-tail of the N protein comprising the amino acid sequence TLLPAADLDDFSKQL which lies within instant SEQ ID NO: 28 (pages 1, 2, 4-5). Tian et al. further teach epitope mapping of the region of the C-tail of the N protein. It is noted that instant SEQ ID NO: 28 spans across three amino acid sequences identified by Tian et al. as epitopes, SARS-CoV-2-N4-7, SARS-CoV-2-N4-8, and SARS-CoV-2-N4-9 (page 3, Fig. 3A).
Tian et al. do not teach treatment of the sample with a serine protease.
However Omir et al. teach an immunoassay method for SARS-CoV-2 detection from a sample, wherein the sample is treated with a serine protease comprising trypsin for the benefit of breaking up and/or lysing any virus present in the sample thereby exposing the target epitope and improving the sensitivity of the assay (¶¶ [0014], [0190]-[0197]).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to have incorporated the trypsin treatment as taught by Omir et al. into the ELISA method taught by Tian et al. for the benefit of breaking up and/or lysing any virus present in the sample thereby exposing the target epitope and improving the sensitivity of the assay. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
One of ordinary skill in the art would have had reasonable expectation of success in incorporating a trypsin treatment step in the ELISA taught by Tian et al. given that the methods of preparing biological samples used for virus detection are well known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
With respect to the recitation in claim 1 of “wherein the peptide fragment comprises the amino acid sequence of SEQ ID NO: 28”, it is noted that this recitation does not do not impart additional method steps to be performed to the method of claim 1, but rather, this recitation refers to an antibody’s target epitope. Given that the epitope sequence taught by Tian et al. lies entirely within instant SEQ ID NO: 28., and given that the epitope of Tian et al. is inherently present where the sequence of SEQ ID NO: 28 is present, skilled artisans would reasonably understand that Tian et al.’s antibody has the functional property of identifying the slightly larger peptide in instant SEQ ID NO: 28. See MPEP 2112.01. I. When the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Further, it should be noted that the instant claim are directed to an immunoassay method and not to an specific antibody. Absent any evidence to the contrary, the method taught by Tian et al., in view of Omir et al. as indicated above renders the method of claim 1 prima facie obvious.
Regarding claim 2, as noted above, Tian et al.’s antibody binds to an epitope comprising the amino acid sequence TLLPAADLDDFSKQL. Given that this sequence lies almost entirely within instant SEQ ID NO: 1 (with the exception of the last two amino acids “QL”) and given that the epitope of Tian et al. is inherently present in the sample where the sequence of SEQ ID NO: 1 is present, skilled artisans would reasonably understand that Tian et al.’s antibody has the functional property of identifying the sequence in instant SEQ ID NO: 1. See MPEP 2112.01. I. When the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Further, it should be noted that the instant claim are directed to an immunoassay method and not to an specific antibody. Absent any evidence to the contrary, the method taught by Tian et al., in view of Omir et al. as indicated above renders the method of claim 2 prima facie obvious.
Regarding claims 3 and 4, Omir et al. teach treatment of a sample comprising for example a mucosal or tissue secretion, mucus, mucus, or saliva with a serine protease (¶¶ [0057], [0190]-[0197]).
Regarding claims 5, 6, 8, Omir et al.’s teach an immunochromatography (LFA) method and an ELISA method wherein in step 1, the sample is contacted with an antibody specific for a SARS-CoV-2 bearing a biotin label thereby forming a first complex. In step 2, the first complex is contacted with a second monoclonal antibody which is bound to a solid phase and wherein the second antibody recognizes a different epitope than the first antibody. Finally, in step 3, a signal is measured (¶¶ [0238]-[0253]). Further, it is noted that it is well within the purview of one of ordinary skill in the art to set up ELISA and/or LFA assays comprising two monoclonal antibodies.
Regarding claim 7, as indicated above, the method of claim 5 is taught by the combinations of the teachings of Tian et al. and Omir et al. wherein one of the antibodies used is capable of detecting the epitopes of instant SEQ ID NO: 1 and SEQ ID NO: 2 given their high sequence identity. See also rejections under 35 USC § 112(b). As noted above, Tian et al.’s antibody binds to an epitope comprising the amino acid sequence TLLPAADLDDFSKQL. Given that the sequence of SEQ ID NO: 2 lies almost entirely within the epitope of Tian et al.’s antibody and given that the epitope of Tian et al. is inherently present in the sample where the sequence of SEQ ID NO: 2 is present, skilled artisans would reasonably understand that Tian et al.’s antibody has the functional property of identifying the sequence in instant SEQ ID NO: 2. See MPEP 2112.01. I. When the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Further, it should be noted that the instant claim are directed to an immunoassay method and not to an specific antibody. Absent any evidence to the contrary, the method taught by Tian et al., in view of Omir et al. as indicated above renders the method of claim 7 prima facie obvious.
Accordingly, claims 1-8 would have been prima facie obvious to one of ordinary skill in the art before the effective filing date, especially in the absence of evidence to the contrary.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARLENE V BUCKMASTER whose telephone number is (703)756-5371. The examiner can normally be reached M-R 8:00 AM - 5:00 PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Thomas J. Visone can be reached on (571)270-0684. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/MARLENE V BUCKMASTER/Examiner, Art Unit 1672
/NICOLE KINSEY WHITE/Primary Examiner, Art Unit 1672
Prosecution Insights