CTFR 18/029,467 CTFR 78206 DETAILED ACTION Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Response Applicant’s response and claims amendment filed on May 05, 206 has been acknowledged. Claims 1, 12, 20-21, 28, 30-32 and 43-44 have been amended. Claims 2-4, 6-11, 13-14, 16-19, 22, 25-26, 29, 34-35, 37-39, 42, 45 have been canceled. Claims 1, 5, 12, 15, 20-21, 28, 30-33, 36, 40-41, 43-44 are pending. Claims 1, 5, 12, 15, 20-21, 23-24, 27- 28, and 30-31 read on the elected species of protein A/G/L are considered. Claims 32-33, 36, 40-41, 43-44 are withdrawn from consideration. Claim Rejections - 35 USC § 102 07-07-aia AIA 07-07 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 – 07-08-aia AIA (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. The rejection of Claim(s) 1, 15, 20, 23, 24, 27-28, 30 and 31 under 35 U.S.C. 102 (a) (1) as being anticipated by US Patent No. 9,442,112B2 to Mehra et al. has been removed necessitated by Applicants’ amendment. Claim Rejections - 35 USC § 102/103 07-20-aia AIA 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. 07-27-aia AIA Claim s 1, 5, 12, 15, 20, 21, 24, 27-28 and 30-31 are still rejected under 35 U.S.C. 102 ( (a) (1 ) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Burbelo et al. (Journal of Infectious Disease, May 19, 2020, Vol. 222, pages 206-213) further in view of Degeling et al. (Anal Chem. 2013 Feb 20;85(5):3006–3012) and Hawkins et al. (Promega Notes, 2005, Number 90, pages 1-14) for claim 27 . In the response, Applicants travers the rejection by asserting while Burbelo discloses using a microtiter filter plate containing protein A/G beads to bind to the antibody (see, e.g., Burbelo page 3 left column), the protein A/G beads capture the antibody on a solid support as shown in Figure 2 of Burbelo. Thus, in Burbelo, the protein A/G beads do not aggregate the a detectably-labeled antigen to form an antibody-fusion protein aggregate as defined in Applicant's specification ("'aggregating agent' refers to an agent that binds to a molecule (e.g., antibody, protein) and is capable of facilitating the accumulation or formulation of tangled clusters, thereby forming an aggregate of the molecules" Specification at page 12:30-33). Thus, Burbelo does not form an antibody-fusion protein aggregate as recited in the currently pending claim 1. Applicants’ argument has been respectfully considered, however, it is not found persuasive because it is so well known that protein A or protein G beads can form an aggregate with these complexes. The beads bind to the Fc region of the antibody, leaving its antigen-binding Fab regions free to capture the hapten-tagged antigen. This forms a Bead–Antibody–Antigen aggregate. Therefore, the rejection is maintained . 07-15 AIA Claim (s) 1, 5, 12, 15, 20, 23, 24, 27-28, 30-31 are still rejected under 35 U.S.C. 102 ( a) (1 ) as being anticipated by or in the alternative, under Haljasmägi et al. (European Journal102/ of Immunology, First published on line, 25, June 2020, https://doi.org/10.1002/eji.202048715 .) further in view of Degeling et al. (Anal Chem. 2013 Feb 20;85(5):3006–3012) . In the response, Applicants traverse the rejection and also argue While Haljasmagi uses protein G to capture the antibody binding agent complex, however, Haljasmagi, does not teach or suggest a method of detecting an antibody through forming a detectably-labeled antigen-fusion protein aggregate at least because the protein G is attached to a solid support (here, Sepharose). Thus, in Haljasmagi the Sepharose beads do not aggregate the a detectably-labeled antigen to form an antibody-fusion protein aggregate as defined in Applicant's specification ("'aggregating agent' refers to an agent that binds to a molecule (e.g., antibody, protein) and is capable of facilitating the accumulation or formulation of tangled clusters, thereby forming an aggregate of the molecules" Specification at page 12:30- 33). Therefore, the antibody binding agent complex does not form a fusion-protein aggregate as recited in claim 1. Degeling is discussed above and does not cure the deficiencies of Haljasmagi. Applicant respectfully requests reconsideration and withdrawal of the Applicants’ argument has been respectfully considered, however, it is not found persuasive because it is so well known that protein A or protein G beads can form an aggregate with these complexes. The beads bind to the Fc region of the antibody, leaving its antigen-binding Fab regions free to capture the hapten-tagged antigen. This forms a Bead–Antibody–Antigen aggregate. In this case, Haljasmägi et al. disclose a sensitive method called Luciferase IP system (LIPS) assay for quantitative detection of antibodies to antigens in their native conformation, wherein the antibody is the one responses to SARS-CoV-2 spike (S) and one to nucleocapsid (N) proteins in COVID-19 patients. First, the SARS-CoV-2 antigens. S1, S2, and N genes were cloned and expressed as a fusion protein with NanoLuc in HEK293 cells. The cell lysates of HEK293 rich in NanoLuc S1, S2 or N fusion proteins were incubated with plasma samples (in 1:40 dilution), which contain antibodies to be detected. The mixture of the antibody and antibody binding agent including S1/NanolLuc. , S2/NanolLuc or N/ /NanolLuc fusion protein of SARS-CoV-2 via its Fab site impolitely/inherently, which is further mixed with protein G Sepharose that is an aggregating forming agent, which allow the antibodies binding Protein G Sepharose through its Fc binding site to capture antibody, whereas the antibody binds to viral antigens via its Fab region hereby forming a complexes aggregates. Therefore, the rejection is maintained. The rejection of Claims 1, 15, 20, 21, 27-28 and 30-31 under 35 U.S.C. 102 (a) (1) as being anticipated or in an alternative obviously by Arai et al. (JOURNAL OF FOERMATION AND BIOENGNEERING , 1998, vol. 86, No. 5, pp. 440-445) for claims 1, 15, 20-21, 28, 31-32 with a further in view of Kain et al. (Expression and detection of Green Fluorescent Protein (GFP) published in 1997, Vol. 63, pp. 305-324) is removed because of the persuasive argument. Conclusion 07-39 AIA THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. 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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. BAO Q. LI Examiner Art Unit 1671 /BAO Q LI/Primary Examiner, Art Unit 1671 Application/Control Number: 18/029,467 Page 2 Art Unit: 1671 Application/Control Number: 18/029,467 Page 3 Art Unit: 1671 Application/Control Number: 18/029,467 Page 4 Art Unit: 1671 Application/Control Number: 18/029,467 Page 5 Art Unit: 1671
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