US 8088376B2
· Chamberlain et al.
· 2012
[cited by applicant]
US 8394925B2
· Chamberlain et al.
· 2013
[cited by applicant]
US 8546543B2
· Lazar
· 2013
[cited by applicant]
US 9803023B2
· Chamberlain et al.
· 2017
[cited by applicant]
US 20150152183A1
· Chamberlain et al.
· 2015
[cited by applicant]
US 20220089752A1
· Liu et al.
· 2022
[cited by applicant]
US 20220403009A1
· Hinton et al.
· 2022
[cited by applicant]
US 20230058162A1
· Hinton et al.
· 2023
[cited by applicant]
US 20230174628A1
· Xie et al.
· 2023
[cited by applicant]
US 20230357367A1
· Borriello et al.
· 2023
[cited by applicant]
EP 2235059B1
· 2015
[cited by applicant]
EP 2444423B1
· 2015
[cited by applicant]
EP 3031913A1
· 2016
[cited by applicant]
EP 2808343B1
· 2019
[cited by applicant]
EP 3872091A1
· 2021
[cited by applicant]
EP 3138853B1
· 2021
[cited by applicant]
EP 4147716A1
· 2023
[cited by applicant]
EP 4188951A2
· 2023
[cited by applicant]
WO 2005012360A2
· 2005
[cited by applicant]
WO 2005054469A1
· 2005
[cited by applicant]
WO 2006051091A1
· 2006
[cited by applicant]
WO 2006053301A2
· 2006
[cited by applicant]
WO 2009058492A2
· 2009
[cited by applicant]
WO 2009086320A1
· 2009
[cited by applicant]
WO 2016050889A1
· 2016
[cited by applicant]
WO 2021156490A2
· 2021
[cited by applicant]
WO 2021158521A1
· 2021
[cited by applicant]
WO 2021173753A1
· 2021
[cited by applicant]
WO 2021186190A1
· 2021
[cited by applicant]
WO 2021203053A1
· 2021
[cited by applicant]
WO 2021207152A1
· 2021
[cited by applicant]
WO 2021211775A1
· 2021
[cited by applicant]
WO 2021226560A1
· 2021
[cited by applicant]
WO 2021247925A1
· 2021
[cited by applicant]
WO 2022010912A1
· 2022
[cited by applicant]
WO 2022010921A1
· 2022
[cited by applicant]
WO 2022015573A2
· 2022
[cited by applicant]
WO 2022026475A2
· 2022
[cited by applicant]
WO 2022046888A1
· 2022
[cited by applicant]
WO 2022047033A1
· 2022
[cited by applicant]
WO 2022140845A1
· 2022
[cited by applicant]
WO 2022159685A2
· 2022
[cited by applicant]
WO 2022204202A1
· 2022
[cited by applicant]
WO 2022251119A2
· 2022
[cited by applicant]
WO 2022271863A1
· 2022
[cited by applicant]
WO 2023028603A2
· 2023
[cited by applicant]
WO 2023037119A1
· 2023
[cited by applicant]
WO 2023215910A1
· 2023
[cited by applicant]
Abbasi J., “Researchers Tie Severe Immunosuppression to Chronic COVID-19 and Virus Variants,” JAMA, vol. 325; No. 20; 2033-2035 (2021).
[cited by applicant]
Agrawal U et al., Severe COVID-19 outcomes after full vaccination of primary schedule and initial boosters: pooled analysis of national prospective cohort studies of 30 million individuals in England, Northern Ireland, …
[cited by applicant]
Al-Lazikani, B. et al., “Standard Conformations for the Canonical Structures of Immunoglobulins,” J. Mol. Biol., vol. 273; 927-948 (1997).
[cited by applicant]
Almagro et al., “Progress and Challenges in the Design and Clinical Development of Antibodies for Cancer Therapy” Front. Immunol., 8:1751, doi: 10.3389/fimmu.2017.01751 (2018).
[cited by applicant]
Almagro, J.C., “Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires,” Journal of Mo…
[cited by applicant]
Andreano, E. et al., “mRNA vaccines and hybrid immunity use different B cell germlines to neutralize Omicron BA.4 and BA.5,” bioRxiv, https://doi.org/10.1101/2022.08.04.502828; 31 pages (2022).
[cited by applicant]
Aschner, C.B. et al., “A multi-specific, multi-affinity antibody platform neutralizes sarbecoviruses and confers protection against SARS-CoV-2 in vivo,” Sci. Transl. Med., vol. 15(697); eadf4549, 13 pages (2023).
[cited by applicant]
Australian Government, “Australian Public Assessment Report for Sotrovimab,” Proprietary Product Name: Xevudy, Sponsor: GlaxoSmithKline Australia Pty Ltd; 58 pages (2021).
[cited by applicant]
Baden, L.R. and Rubin, E.J., “Covid-19—The Search for Effective Therapy,” The New England Journal of Medicine, vol. 382; No. 19; 1851-1852 (2020).
[cited by applicant]
Barnes CO et al., SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature. Dec. 2020;588(7839):682-687. doi: 10.1038/s41586-020-2852-1. Epub Oct. 12, 2020. PMID: 33045718; PMCID: PMC8092461.
[cited by applicant]
Bartsch, Y.C. et al., “Antibody effector functions are associated with protection from respiratory syncytial virus,” Cell, vol. 185; 4873-4886 (2022).
[cited by applicant]
Bassetti M et al., Co-localization of secretogranins/chromogranins with thyrotropin and luteinizing hormone in secretory granules of cow anterior pituitary. J Histochem Cytochem. Sep. 1990;38(9):1353-63. doi: 10.1177/38…
[cited by applicant]
Baud, D. et al., “Real estimates of mortality following COVID-19 infection,” Lancet Infect Dis., vol. 20; No. 7; 773 (2020).
[cited by applicant]
Baum A. et al., “REGN-COV2 antibodies prevent and treat SARSCoV-2 infection in rhesus macaques and hamsters,” Science, vol. 370; No. 6520; 1110-1115 (2020).
[cited by applicant]
Baum, A. et al., “Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies,” Science, vol. 369; 1014-1018 (2020).
[cited by applicant]
Bedouelle et al. (FEBS J. Jan. 2006; 273(1):34-46). (Year: 2006).
[cited by applicant]
Bender Ignacio RA et al., Comparative Pharmacokinetics of Tixagevimab/Cilgavimab (AZD7442) Administered Intravenously Versus Intramuscularly in Symptomatic SARS-CoV-2 Infection. Clin Pharmacol Ther. Dec. 2022;112(6):120…
[cited by applicant]
Boggiano, C. et al., “Update on and Future Directions for Use of Anti-SARS-CoV-2 Antibodies: National Institutes of Health Summit on Treatment and Prevention of COVID-19,” Ann Intern Med, 9 pages (2021).
[cited by applicant]
Böttcher E et al. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J Virol. Oct. 2006; 80(19):9896-8. doi: 10.1128/JVI.01118-06. PMID: 16973594; PMCID: PMC161…
[cited by applicant]
Bournazos S et al., Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity. Cell. Sep. 11, 2014;158(6):1243-1253. doi: 10.1016/j.cell.2014.08.023. PMID: 25215485; PMCID: PMC4167398.
[cited by applicant]
Brown et al. (J Immunol. May 1, 1996; 156(9):3285-91). (Year: 1996).
[cited by applicant]
Bruel, T., “Evidence in support of the use of serum neutralisation data to justify a dose increase of monoclonal antibodies to tackle new variants,” EMA/FDA joint meeting, Institut Pasteur, Virus and Immunity Unit, Oliv…
[cited by applicant]
Bulun, S.E., “Reproductive Physiology,” Physiology and Pathology of the Female Reproductive Axis, Chapter 17; pp. 590-663; Williams Textbook of Endocrinology, Fourteenth Edition (2020).
[cited by applicant]
Burnett, D.L. et al., “Immunizations with diverse sarbecovirus receptor-binding domains elicit SARS-CoV-2 neutralizing antibodies against a conserved site of vulnerability,” Immunity, vol. 54(12); 2908-2921 (2021).
[cited by applicant]
Cao Z et al., VV116 versus Nirmatrelvir-Ritonavir for Oral Treatment of Covid-19. N Engl J Med. Feb. 2, 2023;388(5):406-417. doi: 10.1056/NEJMoa2208822. Epub Dec. 28, 2022. PMID: 36577095; PMCID: PMC9812289.
[cited by applicant]
Cao Z et al., VV116 versus Nirmatrelvir-Ritonavir for Oral Treatment of Covid-19. N Engl J Med. Feb. 2, 2023;388(5):406-417. doi: 10.1056/NEJMoa2208822. Epub Dec. 28, 2022. PMID: 36577095; PMCID: PMC9812289; Supplementa…
[cited by applicant]
Cao Z et al., VV116 versus Nirmatrelvir-Ritonavir for Oral Treatment of Covid-19. N Engl J Med. Feb. 2, 2023;388(5):406-417. doi: 10.1056/NEJMoa2208822. Epub Dec. 28, 2022. PMID: 36577095; PMCID: PMC9812289; The Protoco…
[cited by applicant]
Cao, Y. et al., “B.1.1.529 escapes the majority of SARS-CoV-2 neutralizing antibodies of diverse epitopes,” bioRxiv, 30 pages (2021).
[cited by applicant]
Cao, Y. et al., “BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection,” Nature, vol. 608(7923); 593-602 (2022).
[cited by applicant]
Cao, Y. et al., “Imprinted SARS-CoV-2 humoral immunity induces convergent Omicron RBD evolution,” bioRxiv, 38 pages (2022).
[cited by applicant]
Cao, Y. et al., “Omicron BA.2 specifically evades broad sarbecovirus neutralizing antibodies,” bioRxiv, 39 pages (2022).
[cited by applicant]
Case JB et al., Neutralizing Antibody and Soluble ACE2 Inhibition of a Replication-Competent VSV-SARS-CoV-2 and a Clinical Isolate of SARS-CoV-2. Cell Host Microbe. Sep. 9, 2020;28(3):475-485.e5. doi: 10.1016/j.chom.202…
[cited by applicant]
Case JB et al., Resilience of S309 and AZD7442 monoclonal antibody treatments against infection by SARS-CoV-2 Omicron lineage strains. Nat Commun. Jul. 2, 2022;13(1):3824. doi: 10.1038/s41467-022-31615-7. PMID: 35780162…
[cited by applicant]
Case, B., “Development of a Pan-Sarbecovirus Mucosal Vaccine,” Instructor in Medicine Washington University School of Medicine IDWeek: Next Generation COVID-19 Vaccines, Boston, MA, 16 pages (2023).
[cited by applicant]
Cathcart A.L. et al., “The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2,” BioRxiv, https://doi.org/10.1101/2021.03.09.434607 (2022).
[cited by applicant]
Center for Drug Evaluation and Research, Approval Package for: Application No. 761108Orig1s000, Trade Name: Ultomiris Injection, 300 mg / 30mL (10 mg / mL), retrieved from Internet URL: https://www.google.com/url?sa=t&r…
[cited by applicant]
Centers for Disease Control and Prevention website. COVID-19 vaccines for people who are moderately or severely immunocompromised. Updated Jan. 31, 2023. Accessed Feb. 17, 2023. https://www.cdc.gov/coronavirus/2019-ncov…
[cited by applicant]
Cerutti, G. et al., “Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARSCoV-2 neutralizing antibodies,” Structure, vol. 29(7); 655-663 (2021).
[cited by applicant]
Chan, J.F. et al., “Simulation of the Clinical and Pathological Manifestations of Coronavirus Disease 2019 (COVID-19) in a Golden Syrian Hamster Model: Implications for Disease Pathogenesis and Transmissibility,” Clin I…
[cited by applicant]
Chan, K.K. et al., “Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2,” Science. Sep. 4, 2020;369(6508):1261-1265. doi: 10.1126/science.abc0870. Epub Aug. 4, 2020. PMID: 32753553; PMC…
[cited by applicant]
Chen et al. “CoV-Spectrum: analysis of globally shared SARS-CoV-2 data to identify and characterize new variants”, Bioinformatics 38(6):1735-37 (2022).
[cited by applicant]
Chen, P. et al., “First-in-Human Study of Bamlanivimab in a Randomized Trial of Hospitalized Patients With COVID-19,” Clinical Pharmacology & Therapeutics, vol. 110; No. 6; 1467-1477 (2021).
[cited by applicant]
Chigutsa, E. et al., “A Quantitative Modeling and Simulation Framework to Support Candidate and Dose Selection of Anti-SARS-CoV-2 Monoclonal Antibodies to Advance Bamlanivimab Into a First-in-Human Clinical Trial,” Clin…
[cited by applicant]
Chigutsa, E. et al., “Population Pharmacokinetics and Pharmacodynamics of the Neutralizing Antibodies Bamlanivimab and Etesevimab in Patients With Mild to Moderate COVID-19 Infection,” Clinical Pharmacology & Therapeuti…
[cited by applicant]
Choy, R.K.M. et al., “Controlled Human Infection Models To Accelerate Vaccine Development,” Clinical Microbiology Reviews, vol. 35; Issue 3; 163 pages (2022).
[cited by applicant]
Colman (Research in Immunology, 145:33-36, 1994). (Year: 1994).
[cited by applicant]
Copin, R. et al., “The monoclonal antibody combination REGEN-COV protects against SARS-CoV-2 mutational escape in preclinical and human studies,” Cell, vol. 184(15); 3949-3961 (2021).
[cited by applicant]
Corbett, K.S. et al., “Immune Correlates of Protection by mRNA-1273 Vaccine against SARS-CoV-2 in Nonhuman Primates,” Science, vol. 373; No. 6561; eabj0299; 23 pages (2021).
[cited by applicant]
Correa Giron, C. et al., “On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2,” Virus Research, vol. 285; 198021; 13 pages (202…
[cited by applicant]
Corti et al. “Tackling COVID-19 with neutralizing monoclonal antibodies”, Cell 184(12):3086-3108 (2021).
[cited by applicant]
Crawford JL & McNeilly AS. Co-localisation of gonadotrophins and granins in gonadotrophs at different stages of the oestrous cycle in sheep. J Endocrinol. Aug. 2002;174(2):179-94. doi: 10.1677/joe.0.1740179. PMID: 12176…
[cited by applicant]
Crawford KHD et al., Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays. Viruses. May 6, 2020;12(5):513. doi: 10.3390/v12050513. PMID: 32384820; PMCID: PM…
[cited by applicant]
Credle, J.J. et al., “Unbiased discovery of autoantibodies associated with severe COVID-19 via genome-scale self-assembled DNA-barcoded protein libraries,” Nature Biomedical Engineering, vol. 6(8); 992-1003 (2022).
[cited by applicant]
Cromer D et al., Neutralising antibody titres as predictors of protection against SARS-CoV-2 variants and the impact of boosting: a meta-analysis. Lancet Microbe. Jan. 2022;3(1):e52-e61. doi: 10.1016/S2666-5247(21)00267…
[cited by applicant]
Cuccarese, M.F. et al., “Functional immune mapping with deep-learning enabled phenomics applied to immunomodulatory and COVID-19 drug discovery,” bioRxiv, 24 pages (2020).
[cited by applicant]
Database, RCSB PDB [Online], “7NAB Crystal structure of human neutralizing mAb CV3-25 binding to SARS-CoV-2 S MPER peptide 1140-1165”, 5 pages, PDB DOI: https://doi.org/10.2210/pdb7NAB/pdb (2021).
[cited by applicant]
Davenport, M., “Correlates of protection using a neutralisation approach,” Kirby Institute, 25 pages (2022).
[cited by applicant]
Davis-Gardner, M.E. et al., “mRNA bivalent booster enhances neutralization against BA.2.75.2 and BQ.1.1,” bioRxiv; https://doi.org/10.1101/2022.10.31.514636; 7 pages (2022).
[cited by applicant]
De Gasparo, R.D. et al., “Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice,” Nature, vol. 593(7859); 424-428 (2020).
[cited by applicant]
De Genst et al., “Anti body repertoire development in camelids” Dev Comp Immunol; 30:187-98 (2006).
[cited by applicant]
Dejnirattisai, W. et al., “The antigenic anatomy of SARS-CoV-2 receptor binding domain,” Cell, vol. 184; 2183-2200 (2021).
[cited by applicant]
Dings C et al., Pharmacometric Modeling of the Impact of Azelastine Nasal Spray on SARS-CoV-2 Viral Load and Related Symptoms in COVID-19 Patients. Pharmaceutics. Sep. 27, 2022;14(10):2059. doi: 10.3390/pharmaceutics 14…
[cited by applicant]
Divine, R. et al., “Designed proteins assemble antibodies into modular nanocages,” Science, vol. 372(6537); No. 47; 17 pages (2021).
[cited by applicant]
Dougan, M. et al., “A randomized, placebo-controlled clinical trial of bamlanivimab and etesevimab together in high-risk ambulatory patients with COVID-19 and validation of the prognostic value of persistently high vira…
[cited by applicant]
Dougan, M. et al., “Bebtelovimab, alone or together with bamlanivimab and etesevimab, as a broadly neutralizing monoclonal antibody treatment for mild to moderate, ambulatory COVID-19,” medRxiv, 33 pages (2022).
[cited by applicant]
Dube, S. et al., “Fully vaccinated individuals with immunocompromised conditions are still at increased risk of severe COVID-19 outcomes from the Omicron variant: initial results from Inform, a retrospective health data…
[cited by applicant]
Durán-Pastén ML & Fiordelisio T. GnRH-Induced Ca(2+) Signaling Patterns and Gonadotropin Secretion in Pituitary Gonadotrophs. Functional Adaptations to Both Ordinary and Extraordinary Physiological Demands. Front Endocr…
[cited by applicant]
Edara VV et al., Neutralizing Antibodies Against SARS-CoV-2 Variants After Infection and Vaccination. JAMA. May 11, 2021;325(18):1896-1898. doi: 10.1001/jama.2021.4388. PMID: 33739374; PMCID: PMC7980146.
[cited by applicant]
EMA website. CHMP Assessment Report for Sotrovimab, Dec. 2021. Updated Jan. 12, 2023. Accessed May 22, 2023. https://www.ema.europa.eu/en/documents/assessmentreport/xevudy-epar-public-assessment-report_en.pdf.
[cited by applicant]
Esparza, T.J. and Brody, D.L., “High Affinity Nanobodies Block SARS-CoV-2 Spike Receptor Binding Domain Interaction with Human Angiotensin Converting Enzyme,” bioRxiv, Retrieved from Internet URL: https://www.biorxiv.or…
[cited by applicant]
European Cancer Patient Coalition (ECPC). Joint statement on the protection of immunocompromised patients during the COVID-19 pandemic. Updated Jul. 7, 2022. Accessed Feb. 17, 2023. https://ecpc.org/joint-statement-on-t…
[cited by applicant]
European Medicines Agency, Assessment Report, Evusheld, 155 pages (2022).
[cited by applicant]
European Medicines Agency, CHMP Assessment Report for Xevudy; 120 pages (2021).
[cited by applicant]
Eyal, N. et al., “Human Challenge Studies to Accelerate Coronavirus Vaccine Licensure,” The Journal of Infectious Diseases, vol. 221; 1752-1756 (2020).
[cited by applicant]
Fact Sheet for Health Care Providers, Bamlanivimab and Etesevimab, Eli Lilly and Company, 45 pages (2021).
[cited by applicant]
Fact Sheet for Health Care Providers, casirivimab and imdevimab, Regeneron Pharmaceuticals, Inc, 54 pages (2021).
[cited by applicant]
Fact Sheet for Health Care Providers, Sotrovimab, GlaxoSmithKline LLC, 37 pages (2022).
[cited by applicant]
FDA Briefing Document, “Bezlotoxumab Injection, Meeting of the Antimicrobial Drugs Advisory Committee (AMDAC)” 29 pages (2016).
[cited by applicant]
FDA Briefing Document, “Vaccines and Related Biological Products Advisory Committee Meeting,” EUA amendment request for use of the Moderna COVID-19 Vaccine in children 6 months through 17 years of age, 190 pages (2022).
[cited by applicant]
Fedry, J. et al., “Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11,” Sci. Adv., vol. 7(23); eabf5632, 11 pages (2021).
[cited by applicant]
Fenwick, C. et al., “A highly potent antibody effective against SARS-CoV-2 variants of concern,” Cell Reports, vol. 37(2); 109814; 19 pages (2021).
[cited by applicant]
Fenwick, C. et al., “Patient-derived monoclonal antibody neutralizes SARS-CoV-2 Omicron variants and confers full protection in monkeys,” Nature Microbiology, 33 pages (2022).
[cited by applicant]
Follmann D et al., Examining protective effects of SARS-CoV-2 neutralizing antibodies after vaccination or monoclonal antibody administration. Nat Commun. Jun. 17, 2023;14(1): 23 pages; Supplemental Materials.
[cited by applicant]
Follmann D et al., Examining protective effects of SARS-CoV-2 neutralizing antibodies after vaccination or monoclonal antibody administration. Nat Commun. Jun. 17, 2023;14(1):3605. doi: 10.1038/s41467-023-39292-w. PMID:…
[cited by applicant]
Francica, J.R. et al., “The SARS-CoV-2 monoclonal antibody AZD3152 potently neutralises historical and currently circulating variants,” Presented at the European Congress of Clinical Microbiology and Infectious Diseases…
[cited by applicant]
Francica, J.R. et al., “The SARS-CoV-2 Monoclonal Antibody AZD3152 Potently Neutralizes Historical and Emerging Variants and is Being Developed for the Prevention and Treatment of COVID-19 in High-Risk Individuals,” IDW…
[cited by applicant]
Gau, B.C. et al., “Oligonucleotide mapping via mass spectrometry to enable comprehensive primary structure characterization of an mRNA vaccine against SARS-CoV-2,” Scientific Reports, vol. 13; 9038; 16 pages (2023).
[cited by applicant]
Gauvreau, G.M. et al., “Effects of an Anti-TSLP Antibody on Allergen-Induced Asthmatic Responses,” N. Eng J Med, vol. 370; 2102-2110 (2014).
[cited by applicant]
Genbank, “Lama glama immunoglobulin heavy chain variable region mRNA, partial eds,” Database accession No. MT350284; 2 Pages (2020).
[cited by applicant]
Gilbert PB et al., Immune correlates analysis of the mRNA-1273 COVID-19 vaccine efficacy clinical trial. Science. Jan. 7, 2022;375(6576): 75 pages; Supplemental Material.
[cited by applicant]
Gilbert PB et al., Immune correlates analysis of the mRNA-1273 COVID-19 vaccine efficacy clinical trial. Science. Jan. 7, 2022;375(6576):43-50. doi: 10.1126/science.abm3425. Epub Nov. 23, 2021. PMID: 34812653; PMCID: PM…
[cited by applicant]
Gilbert, P.B. et al., “A Covid-19 Milestone Attained—A Correlate of Protection for Vaccines,” N Engl J Med, vol. 387; No. 24; 2203-2206 (2022).
[cited by applicant]
Gobeil, S. et al., “Structural diversity of the SARS-CoV-2 Omicron spike,” bioRxiv; 35 pages (2022).
[cited by applicant]
Gov.UK, “Winter Coronavirus (COVID-19) Infection Study: estimates of epidemiological characteristics, Dec. 21, 2023,” Retrieved from Internet URL: https://www.gov.uk/government/statistics/winter-coronavirus-covid-19-inf…
[cited by applicant]
Greaney AJ et al., Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition. Cell Host Microbe. Jan. 13, 2021;29(1):44-57.e9. doi: 10.1016/j.chom.2020.11.007. Epub N…
[cited by applicant]
Greaney, A.J. et al., “Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies,” bioRxiv, 35 pages (2021).
[cited by applicant]
Gruell, H. et al., “Antibody-mediated neutralization of SARS-CoV-2,” Immunity, vol. 55(6); 925-944 (2022).
[cited by applicant]
Gupta, A. et al., “Early Treatment for Covid-19 with SARS-CoV-2 Neutralizing Antibody Sotrovimab,” N Eng J Med, vol. 385(21); 1941-1950 (2021).
[cited by applicant]
Gupta, A. et al., “Early Treatment for Covid-19 with SARS-CoV-2 Neutralizing Antibody Sotrovimab,” N Eng J Med, vol. 385(21); The Protocol; 269 pages (2021).
[cited by applicant]
Gutgsell, A.R. et al., “Biosensor-Enabled Deconvolution of the Avidity-Induced Affinity Enhancement for the SARS-CoV-2 Spike Protein and ACE2 Interaction,” Anal Chem, vol. 94; 1187-1194 (2022).
[cited by applicant]
Li, T. et al., “A synthetic nanobody targeting RBD protects hamsters from SARS-CoV-2 infection,” Nature Communication, vol. 12; 4635; 13 pages (2021).
[cited by applicant]
Liu Z et al., Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization. Cell Host Microbe. Mar. 10, 2021;29(3):477-488.e4. doi: 10.1016/j.chom.2021.01.014. Epub Jan. 27, 2…
[cited by applicant]
Liu, H. and Wilson, I.A., “Protective neutralizing epitopes in SARS-CoV-2,” Immunol Rev, vol. 310; No. 1; 76-92 (2022).
[cited by applicant]
Liu, H. et al., “A combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection,” Cell Host & Microbe, vol. 29; 806-818 (2021).
[cited by applicant]
Liu, L. et al., “Anti-spike IgG causes severe acute lung injury by skewing macrophage responses during acute SARS-CoV infection,” JCI Insight, vol. 4; No. 4; e123158; 20 pages (2019).
[cited by applicant]
Liu, L. et al., “Antibodies targeting a quaternary site on SARS-CoV-2 spike glycoprotein prevent viral receptor engagement by conformational locking,” Immunity, vol. 56(10); 2442-2455 (2023).
[cited by applicant]
Liu, L. et al., “Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike,” Nature, vol. 584; 450-456 (2020).
[cited by applicant]
Loo, Y.M. et al., “The SARS-CoV-2 monoclonal antibody combination, AZD7442, is protective in nonhuman primates and has an extended half-life in humans,” Sci. Transl. Med., vol. 14; No. 635; eabl8124; 15 Pages (2022).
[cited by applicant]
Low, J.S. et al., “ACE2 engagement exposes the fusion peptide to pan-coronavirus neutralizing antibodies,” bioRxiv, 56 pages (2022).
[cited by applicant]
Mahoney, K. et al., “1363. Preliminary Safety Results from a Phase 1 First in Human Study of VYD222: an Extended Half-Life Monoclonal Antibody (mAb) in Development for COVID-19 Prevention,” Open Forum Infect Dis. Nov. 2…
[cited by applicant]
Markovic, I. and Savvides, S., “Modulation of Signaling Mediated by TSLP and IL-7 in Inflammation, Autoimmune Diseases, and Cancer,” Frontiers in Immunology, vol. 11; Art. 1557; 19 pages (2020).
[cited by applicant]
Martinez, D.R. et al., “A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice,” Sci. Transl. Med., 10.1126/scitranslmed.abj7125; Jan. 26, 2022; 14(629):eabj7125; 18 pages.
[cited by applicant]
McCallum, M. et al., “Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement,” bioRxiv, 27 pages (2021).
[cited by applicant]
McMahan, K. et al., “Correlates of protection against SARS-CoV-2 in rhesus macaques,” Nature, vol. 590(7847); 630-634; Supp'l Data included (2021).
[cited by applicant]
McNeilly AS et al., The differential secretion of FSH and LH: regulation through genes, feedback and packaging. Reprod Suppl. 2003;61:463-76. PMID: 14635955.
[cited by applicant]
Melanie, P. et al., “Modeling brings additional insights into the kinetics of SARS-CoV-2 neutralizing antibody,” MedRxiv; https://doi.org/10.1101/2021.10.13.21264693; 4 pages (2021).
[cited by applicant]
Menzies-Gow, A. et al., “Tezepelumab in Adults and Adolescents with Severe, Uncontrolled Asthma,” N Eng J Med, vol. 384; 1800-1809 (2021).
[cited by applicant]
Menzies-Gow, A. et al., “Unmet need in severe, uncontrolled asthma: can anti-TSLP therapy with tezepelumab provide a valuable new treatment option?,” Respiratory Research, vol. 21(1); 268; 7 pages (2020).
[cited by applicant]
Meyer, M.C. et al., “Development Approach for Anti-Spike Monoclonal Antibodies to Keep Pace with SARS-CoV-2 Variants,” EMA-FDA Workshop: Efficacy of monoclonal antibodies in the context of rapidly evolving SARS-CoV-2 va…
[cited by applicant]
Miller, J. et al., “Substantial Neutralization Escape by the SARS-CoV-2 Omicron Variant BQ.1.1,” bioRxiv, https://doi.org/10.1101/2022.11.01.514722; 17 pages (2022).
[cited by applicant]
Montgomery, H. et al., “Efficacy and safety of intramuscular administration of tixagevimab-cilgavimab for early outpatient treatment of COVID-19 (Tackle): a phase 3, randomised, double-blind, placebo-controlled trial,” …
[cited by applicant]
Montgomery, H. et al., “Efficacy and safety of intramuscular administration of tixagevimab-cilgavimab for early outpatient treatment of COVID-19 (Tackle): a phase 3, randomised, double-blind, placebo-controlled trial,” …
[cited by applicant]
Moulana A et al., Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA. 1. Nat Commun. Nov. 16, 2022; 13(1):7011. doi: 10.1038/s41467-022-34506-z. PMID: 36384919; PMCID: PMC9668218.
[cited by applicant]
Muñoz-Fontela C et al., Advances and gaps in SARS-CoV-2 infection models. PLoS Pathog. Jan. 13, 2022;18(1):e1010161. doi: 10.1371/journal.ppat.1010161. PMID: 35025969; PMCID: PMC8757994.
[cited by applicant]
Nader A et al., Pharmacokinetics, Safety, and Tolerability of Anti-SARS-CoV-2 Monoclonal Antibody, Sotrovimab, Delivered Intravenously or Intramuscularly in Japanese and Caucasian Healthy Volunteers. Clin Pharmacokinet.…
[cited by applicant]
Naldini L et al., Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector. Proc Natl Acad Sci U S A. Oct. 15, 1996;93(21):11382-8. doi: …
[cited by applicant]
Narkhede, Y.B. et al., “Targeting Viral Surface Proteins through Structure-Based Design,” Viruses, vol. 13; 1320; 18 pages (2021).
[cited by applicant]
Needleman, S.B. and Wunsch, C.D., “A General Method Applicable to the Search of Similarities in the Amino Acid Sequence of Two Proteins,” J. Mol. Biol., vol. 48; 443-453 (1970).
[cited by applicant]
Nicol L et al., Differential secretion of gonadotrophins: investigation of the role of secretogranin II and chromogranin A in the release of LH and FSH in LbetaT2 cells. J Mol Endocrinol. Apr. 2004;32(2):467-80. doi: 10…
[cited by applicant]
NIH COVID-19 Treatment Guidelines: Anti-SARS-CoV-2 Monoclonal Antibodies: http://www.covid19treatmentguidelines.nih.gov/therapies/anti-sars-cov-2-antibody-products/anti-sars-cov-2-monoclonal-antibodies (date unavailable…
[cited by applicant]
O'Brien, M.P. et al., “Subcutaneous REGEN-COV Antibody Combination to Prevent Covid-19,” The New England Journal of Medicine, vol. 385(13); 1184-1195 (2021).
[cited by applicant]
Ozawa, H. et al., “The Granin Family—Its Role in Sorting and Secretory Granule Formation,” Cell Structure and Function, vol. 20; 415-420 (1995).
[cited by applicant]
Pantaleo, G. et al., “Antibodies to combat viral infections: development strategies and progress,” Nat Rev Drug Discov., Sep. 2022;21(9):676-696. doi: 10.1038/s41573-022-00495-3. Epub Jun. 20, 2022. PMID: 35725925; PMCI…
[cited by applicant]
Park, Y. et al., “Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry,” Science, 10.1126/science.abm8143; 14 pages (2022).
[cited by applicant]
Park, Y. et al., “Imprinted antibody responses against SARS-CoV-2 Omicron sublineages,” bioRxiv, 68 pages (2022).
[cited by applicant]
Pearson, W.R. and Lipman, D.J., “Improved tools for biological sequence comparison,” Proc. Natl. Acad. Sci., vol. 85; 2444-2448 (1988).
[cited by applicant]
Perez, J.L., “Use of neutralizing antibody or PK/IC50 threshold to expedite clinical development for prophylactic monoclonal antibodies,” EMA/FDA workshop on monoclonal antibodies against SARS-CoV-2, AstraZeneca, Vaccin…
[cited by applicant]
Pérez-Vargas J et al., Discovery of lead natural products for developing pan-SARS-CoV-2 therapeutics. Antiviral Res. Jan. 2023;209:105484. doi: 10.1016/j.antiviral.2022.105484. Epub Dec. 8, 2022. Erratum in: Antiviral R…
[cited by applicant]
Petkova SB et al., Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease. Int Immunol. Dec. 2006; 18(12):1759-…
[cited by applicant]
Pinto et al. “Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody”, Nature 583(7815): 290-95 (2020).
[cited by applicant]
Pinto, D. et al., “Broad betacoronavirus neutralization by a stem helix-specific human antibody,” Science, Supplemental Materials, 37 pages (2021).
[cited by applicant]
Pinto, D., et al., “Broad betacoronavirus neutralization by a stem helix-specific human antibody”, Coronavirus, vol. 373, No. 6559, Sep. 3, 2021, pp. 1109-1116.
[cited by applicant]
Polack, F.P. et al., “Safety and Efficacy of the BNT162b2 mRNA Covid-19 Vaccine,” N. Engl. J. Med, vol. 383; No. 27; 2603-2615 (2020).
[cited by applicant]
Portal-Celhay, C. et al., “Phase 2 dose-ranging study of the virologic efficacy and safety of the combination COVID-19 antibodies casirivimab and imdevimab in the outpatient setting,” medRxiv; https://doi.org/10.1101/20…
[cited by applicant]
Pradhan, A. et al., “Affinity maturation of cross-reactive CR3022 antibody against the receptor binding domain of SARS-CoV-2 via in silico site-directed mutagenesis,” Retrieved from Internet URL: http://assets.researchs…
[cited by applicant]
Prévost J et al., Cross-Sectional Evaluation of Humoral Responses against SARS-CoV-2 Spike. Cell Rep Med. Oct. 20, 2020;1(7):100126. doi: 10.1016/j.xcrm.2020.100126. Epub Sep. 30, 2020. PMID: 33015650; PMCID: PMC7524645.
[cited by applicant]
Pymm, P. et al., “Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice,” PNAS, vol. 118; No. 19; e2101918118, 12 pages (2021).
[cited by applicant]
Quanterix, The Science of Precision Health, “Simoa® SARS CoV-2 N Protein Advantage Kit: HD-X Data Sheet,” Quanterix Corporation, Doc Template-0061 03; DS-0528 01DS-0528; 2 pages (2020).
[cited by applicant]
Quanterix, The Science of Precision Health, “Simoa® SARS-CoV-2 Spike IgG Advantage Kit: HD-X Data Sheet,” Quanterix Corporation, Doc Template-0061 03; DS-0521 01DS-0521; 3 pages (2020).
[cited by applicant]
Rambaut, A. et al., “A dynamic nomenclature proposal for SARSCoV-2 lineages to assist genomic epidemiology,” Nat Microbiol., vol. 5; No. 11; 1403-1407 (2020).
[cited by applicant]
Chen, J. et al., “Review of COVID-19 Antibody Therapies,” Cornell University Library, New York, 30 pages (2020).
[cited by applicant]
Ju, B. et al., “Potent human neutralizing antibodies elicited by SARS-CoV-2 infection,” retrieved from Internet URL: http://www.biorxiv.org/content/10.1101/2020.03.21.990770V2.full.pdf; 42 Pages; Retrieved on Oct. 6, 20…
[cited by applicant]
Magar, R. et al., “Potential Neutralizing Antibodies Discovered for Novel Corona Virus Using Machine Learning,” Cornell University Library, New York, 35 pages (2020).
[cited by applicant]
Park, T. et al., “Spike protein binding prediction with neutralizing antibodies of SARS-CoV-2” retrieved from Internet URL: http://www.biorxiv.org/content/10.1101/2020.02.22.951178v1.full.pdf; 22 Pages; Retrieved on Jun…
[cited by applicant]
Pinto, D. et al., “Structural and functional analysis of a potent sarbecovirus neutralizing antibody,” retrieved from Internet URL: http://www.biorxiv.org/content/10.1101/2020.04.07.023903v3.full.pdf; 28 pages (2020).
[cited by applicant]
Planas, D. et al., “Reduced sensitivity of SARA-CoV-2 variant Delta to antibody neutralization,” Nature, 22 pages (2021).
[cited by applicant]
Notification of Transmittal of the International Search Report and the Written Opinion for International Application No. PCT/US2021/040533, mailed Oct. 22, 2021.
[cited by applicant]
Walser, M. et al., Highly potent anti-SARS-CoV-2 multi-DARPin therapeutic candidates, bioRxiv, 39 pages (2020).
[cited by applicant]
Wang, C. et al., “A human monoclonal antibody blocking SARS-CoV-2 infection,” bioRxiv, 24 pages (2020).
[cited by applicant]
Wang, C. et al., “A human monoclonal antibody blocking SARS-CoV-2 infection,” Nature Communications, vol. 11; 2251; 6 pages (2020).
[cited by applicant]
Wang, E.Y. et al., “Diverse functional autoantibodies in patients with COVID-19,” Nature, Jul. 2021; 595(7866):283-288. doi: 10.1038/s41586-021-03631-y. Epub May 19, 2021. PMID: 34010947.
[cited by applicant]
Wang, N. et al., “Subunit Vaccines Against Emerging Pathogenic Human Coronaviruses,” Frontiers in Microbiology, vol. 11; Article 298, 19 pages (2020).
[cited by applicant]
Wang, Q. et al., Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants Cell, vol. 186; 279-286 (2023).
[cited by applicant]
Wang, Z. et al., “Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins,” Immunity, vol. 55; 1-15, 24 pages (2022).
[cited by applicant]
Wang, Z. et al., “Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins,” Immunity, vol. 55; 1-15, 24 pages; Supplemental Information (2022).
[cited by applicant]
Weinreich DM et al., REGN-COV2, a Neutralizing Antibody Cocktail, in Outpatients with Covid-19, N Engl J Med. 384(3):238-251 (2021).
[cited by applicant]
Westendorf, K. et al., “LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants,” Cell Rep., vol. 39; No. 7; 110812; 72 Pages (2022).
[cited by applicant]
WHO website. WHO Coronavirus (COVID-19) Dashboard With Vaccination Data. Updated Feb. 17, 2023. Accessed Feb. 19, 2023. https://covid19.who.int/.
[cited by applicant]
Worzner, K. et al., “Adjuvanted SARS-CoV-2 spike protein elicits neutralizing antibodies and CD4 T cell responses after a single immunization in mice,” EBioMedicine, vol. 63; 103197; 9 pages (2021).
[cited by applicant]
Wrapp, D. et al., “Crystal structure of the SARS-CoV-1 RBD bound by the cross-reactive single-domain antibody SARS VHH-72,” Protein Data Bank (PDB) Accession No. 6WAQ, retrieved from Internet URL: https://www.rcsb.org/s…
[cited by applicant]
Wrapp, D. et al., “Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Doman Camelid Antibodies,” Cell, vol. 181; 1004-1015 (2020).
[cited by applicant]
Wrapp, D., et al., “Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation”, Science, vol. 367, No. 6483, Feb. 19, 2020, pp. 1260-1263.
[cited by applicant]
Wu H et al., Development of motavizumab, an ultra-potent antibody for the prevention of respiratory syncytial virus infection in the upper and lower respiratory tract. J Mol Biol. May 4, 2007;368(3):652-65. doi: 10.1016…
[cited by applicant]
Wu, Y. et al., “A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2,” Science, vol. 368; 1274-1278 (2020).
[cited by applicant]
Wu, Y. et al., “Identification of Human Single-Domain Antibodies against SARS-CoV-2,” Cell Host & Microbe, vol. 27; 891-898 (2020).
[cited by applicant]
Xiang, Y. et al., Versatile, Multivalent Nanobody Cocktails Efficiently Neutralize SARS-CoV-2, bioRxiv, Retrieved from Internet URL: https://www.biorxiv.org/content/10.1101.2020.08.24.264333v3.full.pdf; 34 Pages (2020).
[cited by applicant]
Xu, J. et al., “Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants,” Nature, vol. 595; 278-282 (2021).
[cited by applicant]
Yamin R et al., Fc-engineered antibody therapeutics with improved anti-SARS-CoV-2 efficacy. Nature. Nov. 2021;599(7885):465-470. doi: 10.1038/s41586-021-04017-w. Epub Sep. 21, 2021. PMID: 34547765; PMCID: PMC9038156.
[cited by applicant]
Yang, D. et al., “Comparison of biosensor platforms in the evaluation of high affinity antibody-antigen binding kinetics,” Analytical Biochemistry, vol. 508; 78-96 (2016).
[cited by applicant]
Yonesi, M. and Rezazadeh, A., “Plants as a prospective source of natural anti-viral compounds and oral vaccines against COVID-19 coronavirus,” preprint, https://doi.org/10.20944/preprints202004.0321.v1; 31 pages (2020).
[cited by applicant]
Yoshinaga et al., “Ig L-chain Shuffling for Affinity Maturation of Phage Library-derived Human Anti-human MCP-1 Antibody Blocking its Chemotactic Activity” J. Biochem; 143:593-601 (2008).
[cited by applicant]
Young, S. and Linville-Engler, G., “INVIVYD Submits Request for Emergency Use Authorization (EUA) to U.S. FDA for VYD222FOR the Pre-Exposure Prevention of COVID-19 in Immunocompromised Adults Andadolescents,” Retrieved …
[cited by applicant]
Yuan M et al., A broad and potent neutralization epitope in SARS-related coronaviruses. Proc Natl Acad Sci U S A. Jul. 19, 2022;119(29):e2205784119. doi: 10.1073/pnas.2205784119. Epub Jun. 29, 2022. PMID: 35767670; PMCI…
[cited by applicant]
Yuan, M. et al., “A higly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV,” Science, vol. 368; 4 pages (2020).
[cited by applicant]
Zalevsky, J. et al., “Enhanced antibody half-life improves in vivo activity,” Nat. Biotechnol., vol. 28; No. 2; 157-159 (2010).
[cited by applicant]
Zhang A et al., Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection. Nat Rev Immunol. Jun. 2023;23(6):381-396. doi: 10.1038/s41577-022-00813-1. Epub Dec. 19, 2022. PMID: 36536068; PMC…
[cited by applicant]
Zhang, F. et al., “Human anti-ACE2 monoclonal antibodies as pan-sarbecovirus prophylactic agents,” bioRxiv; https://doi.org/10.1101/2022.08.24.505169; 47 pages (2022).
[cited by applicant]
Zhang, H. et al., “Algorithm for Optimized mRNA Design Improves Stability and Immunogenicity,” Nature, https://doi.org/10.1038/s41586-023-06127-z, 52 pages (2023).
[cited by applicant]
Zhao, E. et al., “The Secretogranin II-Derived Peptide Secretoneurin Stimulates Luteinizing Hormone Secretion from Gonadotrophs,” Endocrinology, vol. 150; No. 5; 2273-2282 (2009).
[cited by applicant]
Zhao, F. et al., “Broadening a SARS-CoV-1 neutralizing antibody for potent SARS-CoV-2 neutralization through directed evolution,” Retrieved from Internet URL: http://biorxiv.org/content/10.1101.2021.05.29.443900v1.full.…
[cited by applicant]
Zhou et al. “A general-purpose protein design framework based on mining sequence-structure relationships in known protein structures”, Proc Natl Acad Sci U S A. 117(2):1059-68 (2020).
[cited by applicant]
Zhou, D. et al., “Evidence of escape of SARS-CoV-2 variant B. 1.351 from natural and vaccine-induced sera,” Cell, vol. 184(9); 2348-2361 (2021).
[cited by applicant]
Zhou, P., et al., “A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection”, Science Translational Medicine, vol. 14, No. 637, Mar. 23, 2022, 2 pa…
[cited by applicant]
Zhou, Q., “Considerations Regarding Assessment of A Modified Monoclonal Antibody (mAb) Product Related to A Prototype mAb Product in Addressing Emerging SARS-COV-2 Variants—A CMC Perspective,” Presentation; EMA-FDA Work…
[cited by applicant]
Ziegler, C.G.K. et al., “SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets Across Tissues,” Cell, vol. 181; 1016-1035 (2020).
[cited by applicant]
Zost SJ et al., Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature. Aug. 2020;584(7821):443-449. doi: 10.1038/s41586-020-2548-6. Epub Jul. 15, 2020. PMID: 32668443; PMCID: PMC7584396.
[cited by applicant]
Zupancic, J.M. et al., “Engineered Multivalent Nanobodies Potently and Broadly Neutralize SARS-CoV-2,” Advanced Therapeutics, vol. 4; 2100099; 9 Pages (2021).
[cited by applicant]
Rappazzo CG et al., Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody. Science. Feb. 19, 2021;371(6531):823-829. doi: 10.1126/science.abf4830. Epub Jan. 25, 2021. PMID: 33495…
[cited by applicant]
Rockett, R. et al., “Resistance Mutations in SARS-CoV-2 Delta Variant after Sotrovimab Use,” N Engl J Med, vol. 386; No. 15; 4 pages (2022).
[cited by applicant]
Rudikoff et al. “Single amino acid substitution altering antigen-binding specificity”, Proceedings of the National Academy of Sciences, National Academy of Sciences, vol. 79, Mar. 1, 1982 (Mar. 1, 1982), p. 1979-1983, X…
[cited by applicant]
Rujas, E. et al., “Multivalency transforms SARS-CoV-2 antibodies into ultrapotent neutralizers,” Nature Communications, vol. 12(1); 3661; 12 pages (2021).
[cited by applicant]
Sauer, M. M., et al., “Structural basis for broad coronavirus neutralization”, Nature Structural & Molecular Biology, vol. 28, 2021, pp. 478-486.
[cited by applicant]
Saunders, K.O., “Conceptual Approaches to Modulating Antibody Effector Functions and Circulation Half-Life,” Front Immunol., vol. 10; 1296 (2019).
[cited by applicant]
Saunders, K.O., “Developing a Neutralizing Antibody Vaccine for Pandemic and Pre-Emergent Coronaviruses,” Duke University School of Medicine, IDWeek, 31 pages (2023).
[cited by applicant]
Schepens, B. et al., “An affinity-enhanced, broadly neutralizing heavy chain-only antibody protects against SARS-CoV-2 infection in animal models,” Sci Transl Med., vol. 13; eabi7826; 18 pages (2021).
[cited by applicant]
Schoof, M. et al., “An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation,” bioRxiv, Retrieved from Internet URL: https://www.biorxiv.org/content/10.1101.2020.08.08.238…
[cited by applicant]
Service, R.F., “New antibodies that the coronavirus can't elude,” Science, vol. 380; Issue 6647; 779-780 (2023).
[cited by applicant]
Seydoux E et al., Analysis of a SARS-CoV-2-Infected Individual Reveals Development of Potent Neutralizing Antibodies with Limited Somatic Mutation. Immunity. Jul. 14, 2020;53(1):98-105.e5. doi: 10.1016/j.immuni.2020.06.…
[cited by applicant]
Sheridan, D. et al., “Design and preclinical characterization of ALXN1210: A novel anti-C5 antibody with extneded duration of action,” PLoS One, vol. 13; No. 4; e0195909; 15 pages (2018).
[cited by applicant]
Sherman, A.C. et al., “The Future of Flu: A Review of the Human Challenge Model and Systems Biology fort Advancement of Influenza Vaccinology,” Frontiers in Cellular and Infection Microbiology, vol. 9; Article 107; 9 pa…
[cited by applicant]
Sheward, D.J. et al., “Structural basis of Omicron neutralization by affinity-matured public antibodies,” bioRxiv, 24 pages (2022).
[cited by applicant]
Shi, R. et al., “A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2,” Nature, vol. 584; No. 7819; 120-124 (2020).
[cited by applicant]
Sia, S.F. et al., “Pathogenesis and transmission of SARS-CoV-2 in golden hamsters,” Nature, vol. 583; 834-837; Supp'l Data included (2020).
[cited by applicant]
Smith, T.F. and Waterman, M.S., “Comparison of Biosequences,” Advances in Applied Mathematics, vol. 2; 482-489 (1981).
[cited by applicant]
Snijder J et al., An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus. Immunity. Apr. 17, 2018;48(4):799-811.e9. doi: 10.1016/j.immuni.2…
[cited by applicant]
Song et al. “Cytokine storm induced by SARS-CoV-2”, Clin Chim Acta. 509:280-7 (2020).
[cited by applicant]
Song, Y. et al., “Effects of Secretoneurin and Gonadotropin-Releasing Hormone Agonist on the Spawning of Captive Greater Amberjack (
[cited by applicant]
Stadler, E. et al., “Determinants of passive antibody effectiveness in SARS-CoV-2 infection,” medRxiv; https://doi.org/10.1101/2022.03.21.22272672; 28 pages (2022).
[cited by applicant]
Stadler, E. et al., “Monoclonal antibody levels and protection from COVID-19,” medRxiv; https://doi.org/10.1101/2022.11.22.22282199; 26 pages (2022).
[cited by applicant]
Stamatatos L et al., mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection. Science. Mar. 25, 2021;372(6549):1413-8. doi: 10.1126/science.abg9175. Epub ahead of print. PMID: 3376…
[cited by applicant]
Starr, T.N. et al., “SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape,” Nature, https://doi.org/10.1038/s41586-021-03807-6; 36 pages (2021).
[cited by applicant]
Stryer, L., Biochemistry, 4th edition, W. H. Freeman and Company, 1995, pp. 18-23.
[cited by applicant]
Sun, B., “Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2,” Nature Portfolio, Nature Microbiology, Reviewer comments & Editors Decisions, 55 pages, No Date Given.
[cited by applicant]
Sun, D. et al., “Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting diverse and conserved epitopes,” Nature Communications, vol. 12; 4676; 14 pages (2021).
[cited by applicant]
Sun, X. et al., “Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2,” Nature Microbiology, vol. 7; 1063-1074 (2022).
[cited by applicant]
Sun, X. et al., “Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2,” Nature Microbiology, vol. 7; 1063-1074; Supplemental Data (2022).
[cited by applicant]
Tabynov, K. et al., “An adjuvanted subunit SARS-CoV-2 spike protein vaccine provides protection against Covid-19 infection and transmission,” npj Vaccines, vol. 7; No. 24; 10 pages (2022).
[cited by applicant]
Tao, K. et al., “The biological and clinical significance of emerging SARS-CoV-2 variants,” Nature Reviews Genet., vol. 22; 757-773 (2021).
[cited by applicant]
Ter Meulen J et al., Human monoclonal antibody as prophylaxis for SARS coronavirus infection in ferrets. Lancet. Jun. 26, 2004;363(9427):2139-41. doi: 10.1016/S0140-6736(04)16506-9. PMID: 15220038; PMCID: PMC7112500.
[cited by applicant]
Ter Meulen, J. et al., “Human Monoclonal Antibody Combination against SARA Coronavirus: Synergy and Coverage of Escape Mutants,” PloS; vol. 3; Issue 7; e237; 9 pages (2006).
[cited by applicant]
Tian, X. et al., “Potent binding of 2019 novel coronavirus spike protein by a SARA coronavirus-specific human monoclonal antibody,” Emerging Microbes & Infections, vol. 9; 4 pages (2020).
[cited by applicant]
Tortorici et al. “Broad sarbecovirus neutralization by a human monoclonal antibody”, Nature. Sep. 2021;597 (7874):103-108. doi: 10.1038/s41586-021-03817-4. Epub Jul. 19, 2021 PMID: 34280951.
[cited by applicant]
Tortorici et al. “Broad sarbecovirus neutralization by a human monoclonal antibody”, Nature. Sep. 2021;597 (7874):103-108. doi: 10.1038/s41586-021-03817-4. Epub Jul. 19, 2021 PMID: 34280951; Suppl. info.
[cited by applicant]
Tortorici, M.A. et al., “Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms,” Science, vol. 370; 950-957 (2020).
[cited by applicant]
Trudeau VL et al., Is secretoneurin a new hormone? Gen Comp Endocrinol. Jan. 1, 2012;175(1):10-8. doi: 10.1016/j.ygcen.2011.10.008. Epub Oct. 20, 2011. PMID: 22036841.
[cited by applicant]
Turelli, P. et al., “P2G3 human monoclonal antibody neutralizes SARS-CoV-2 Omicron subvariants including BA.4 and BA.5 and Bebtelovimab escape mutants,” bioRxiv, 15 pages (2022).
[cited by applicant]
U.S. Department of Health and Human Services, “COVID-19: Developing Drugs and Biological Products for Treatment or Prevention Guidance for Industry,” Center for Drug Evaluation and Research (CDER); Center for Biologics …
[cited by applicant]
U.S. Department of Health and Human Services, “Development of Monoclonal Antibody Products Targeting SARS-CoV-2 for Emergency Use Authorization Guidance for Industry,” Center for Drug Evaluation and Research (CDER); 14 …
[cited by applicant]
Ullah, I. et al., “Live imaging of SARS-CoV-2 infection in mice reveals that neutralizing antibodies require Fc function for optimal efficacy,” Immunity, vol. 54; 2143-2158 (2021).
[cited by applicant]
Ullah, I. et al., “Live imaging of SARS-CoV-2 infection in mice reveals that neutralizing antibodies require Fc function for optimal efficacy,” Immunity, vol. 54; 2143-2158; Supplemental Information (2021).
[cited by applicant]
Vajdos et al. (J Mol Biol. Jul. 5, 2002; 320(2):415-28). (Year: 2002).
[cited by applicant]
Van Egerens, D. et al., “Risk of evolutionary escape from neutralizing antibodies targeting SARS-CoV-2 spike protein,” medRxiv, https://doi.org/10.1101/2020.11.17.20233726; 28 pages (2020).
[cited by applicant]
Veesler, D. et al., “SARS-CoV-2 S glycoprotein in complex with S2X259 Fab,” Worldwide Protein Data Bank, Full wwPDB EM Validation Report; EMDB ID: EMD-24347, PDB ID: 7RA8; 76 pages (2022).
[cited by applicant]
Verstraete, K. et al., “Structure and antagonism of the receptor complex mediated by human TSLP in allergy and asthma,” Nature Communications, vol. 8; 14937; 17 pages (2017).
[cited by applicant]
Vir Biotechnology, “Vir Biotechnology Announces Topline Data from Phase 2 Peninsula Trial Evaluating VIR-2482 for thePrevention of Seasonal Infl uenza A Illness,” Retrieved from Internet URLhttps://investors.vir.bio/new…
[cited by applicant]
Walker KW et al., Pharmacokinetic comparison of a diverse panel of non-targeting human antibodies as matched IgG1 and IgG2 isotypes in rodents and non-human primates. PLoS One. May 23, 2019;14(5):e0217061. doi: 10.1371/…
[cited by applicant]
Walker, L.M. and Burton, D.R., “Passive immunotherapy of viral infections: ‘super-antibodies’ enter the fray,” Nature Reviews, vol. 18; 297-308 (2018).
[cited by applicant]
Haagmans, B.L. et al., “SARS-CoV-2 Neutralizing Human Antibodies Protect Against Lower Respiratory Tract Disease in a Hamster Model,” Journal of Infectious Diseases, vol. 223(12):2020-2028 (2021).
[cited by applicant]
Hansen, J. et al., “Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail,” Science, vol. 369(6506); 1010-1014 (2020).
[cited by applicant]
Haraya, K. et al., “Translational Approach for Predicting Human Pharmacokinetics of Engineered Therapeutic Monoclonal Antibodies with Increased FcRn-Binding Mutations,” BioDrugs, vol. 37; No. 1; 99-108 (2023).
[cited by applicant]
Harpaz R. et al., “Prevalence of Immunosuppression Among US Adults, 2013,” JAMA, vol. 316; No. 23; 2547-2548 (2016).
[cited by applicant]
Hastie, K.M. et al., “Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study,” Science, 10.1126/science.abh2315; 13 pages (2021).
[cited by applicant]
Hastie, K.M. et al., “Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study,” Science, 10.1126/science.abh2315; 13 pages; Supplemental Information (2021).
[cited by applicant]
Hie, B.L. et al., “Efficient evolution of human antibodies from general protein language models,” Nature Biotechnology, https://doi.org/10.1038/s41587-023-01763-2; 26 pages (2023).
[cited by applicant]
Highlights of Emergency Use Authorization, Bebtelovimab, 21 pages (2022).
[cited by applicant]
Highlights of Emergency Use Authorization, Evusheld, 27 pages (2021).
[cited by applicant]
Highlights of Emergency Use Authorization, Evusheld; 30 pages; Revised Jan. 2023.
[cited by applicant]
Hirsch C. et al., “SARS-CoV-2-neutralising monoclonal antibodies to prevent COVID-19,” Cochrane Database Syst Rev., Issue 6; Art No. CD014945; 106 pages (2022).
[cited by applicant]
Hirsch C. et al., “SARS-CoV-2-neutralising monoclonal antibodies to prevent COVID-19,” Cochrane Database Syst Rev., vol. 6; Issue 6; Art No. CD014945; 89 pages (2022).
[cited by applicant]
Holland et al., ACTIV-3—Therapeutics for Inpatients with COVID-19 (TICO) Study Group. Tixagevimab-cilgavimab for treatment of patients hospitalised with COVID-19: a randomised, double-blind, phase 3 trial. Lancet Respir…
[cited by applicant]
Hu, D. and Irving, A. T., “Massively-multiplexed epitope mapping techniques for viral antigen discovery,” Front. Immunol., vol. 14; 1192385; 13 pages (2023).
[cited by applicant]
Hua L et al., MEDI4893* Promotes Survival and Extends the Antibiotic Treatment Window in a
[cited by applicant]
Huang, Y. et al., “Identification of a conserved neutralizing epitope present on spike proteins from all highly pathogenic coronaviruses,” bioRxiv, 27 (2021).
[cited by applicant]
Huang, Y. et al., “Identification of a conserved neutralizing epitope present on spike proteins from all highly pathogenic coronaviruses,” bioRxiv, 27; Supplemental Information (2021).
[cited by applicant]
Huo, J. et al., “Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2,” Nature Structural and Molecular Biology, vol. 27; 846-854 (2020).
[cited by applicant]
Hurlburt N.K. et al., “Structural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit,” Commun Biol., vol. 5; No. 1; 342; 13 Pages (2022).
[cited by applicant]
Ingraham et al. “Generative models for graph-based protein design”, 33rd Conference on Neural Information Processing Systems (Neurl PS 2019), Vancouver, Canada.
[cited by applicant]
International Preliminary Report on Patentability received for PCT Patent Application No. PCT/US2021/040533, mailed on Jan. 19, 2023, 9 pages.
[cited by applicant]
Irvin SC et al., REGEN-COV® antibody cocktail bioanalytical strategy: comparison of LC-MRM-MS and immunoassay methods for drug quantification. Bioanalysis. Dec. 2021;13(24):1827-1836. doi: 10.4155/bio-2021-0190. Epub No…
[cited by applicant]
Isa F et al., Repeat subcutaneous administration of casirivimab and imdevimab in adults is well-tolerated and prevents the occurrence of COVID-19. Int J Infect Dis. Sep. 2022;122:585-592. doi: 10.1016/j.ijid.2022.06.045…
[cited by applicant]
Ishino, T. et al., “Engineering a Monomeric Fc Domain Modality by N-Glycosylation for the Half-life Extension of Biotherapeutics,” Journal of Biological Chemistry, vol. 288; No. 23; 16529-16537 (2013).
[cited by applicant]
Janeway et al., The Recognition of Antigen, Immunobiology, 3rd edition, Garland Publishing Inc., 1997, pp. 3:1-3:11.
[cited by applicant]
Jennewein M.F. et al., “Isolation and characterization of crossneutralizing coronavirus antibodies from COVID-19+ subjects,” Cell Rep. vol. 36; No. 2; 109353; 22 Pages (2021).
[cited by applicant]
Jette, C.A. et al., “Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies,” Cell Reports, vol. 36; 109760; 23 pages (2021).
[cited by applicant]
Jiang, N. et al., “Bivalent mRNA vaccine improves antibody-mediated neutralization of many SARS-CoV-2 Omnicron lineage variants,” bioRxiv; 21 pages (2023).
[cited by applicant]
Jiang, W. et al., “Characterization of MW06, a human monoclonal antibody with cross-neutralization activity against both SARS-CoV-2 and SARS-CoV,” MABS, vol. 13; No. 1; e1953683; 12 pages (2021).
[cited by applicant]
Jones, B.E. et al., “The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates,” Sci. Transl. Med., vol. 13; eabf1906; 17 pages (2021).
[cited by applicant]
JP Morgan Healthcare Conference, Regeneron; Retrieved from Internet URL: https://investor.regeneron.com/events/event-details/41st-annual-jp-morgan-healthcare-conference; 37 pages; Retrieved on Jan. 29, 2024.
[cited by applicant]
Kaku Y et al., Virological characteristics of the SARS-CoV-2 JN. 1 variant. Lancet Infect Dis. Feb. 2024;24(2):e82. doi: 10.1016/S1473-3099(23)00813-7. Epub Jan. 3, 2024. PMID: 38184005.
[cited by applicant]
KC, B.B. et al., “A machine learning platform to estimate anti-SARS-CoV-2 activities,” Nature Machine Intelligence, https://doi.org/10.1038/s42256-021-00335-w; 9 pages (2021).
[cited by applicant]
Khoury DS et al., Neutralizing antibody levels are highly predictive of immune protection from symptomatic SARS-CoV-2 infection. Nat Med. Jul. 2021;27(7):1205-1211. doi: 10.1038/s41591-021-01377-8. Epub May 17, 2021. PM…
[cited by applicant]
Killingley, B. et al., “Safety, tolerability and viral kinetics during SARS-CoV-2 human challenge in young adults,” Nature Medicine, vol. 28, 1031-1041 (2022).
[cited by applicant]
Knierman, M.D. et al., “The Human Leukocyte Antigen Class II Immunopeptidome of the SARS-CoV-2 Spike Glycoprotein,” Cell Reports, vol. 33; 1 08454; 15 pages (2020).
[cited by applicant]
Kreuzberger N. et al., “SARS-CoV-2-neutralising monoclonal antibodies for treatment of COVID-19,” Cochrane Database Syst Rev, vol. 9; No. 9 229 pages (2021).
[cited by applicant]
Kunik, V. et al., “Paratome: an online tool for systematic identification of antigen-binding regions in antibodies based on sequence or structure,” Nucleic Acids Research, vol. 40; W521-W524 (2012).
[cited by applicant]
Kupferschmidt, K., “Evolving threat,” Science, vol. 373; No. 6557; 844-849 (2021).
[cited by applicant]
Kurasaki, H. et al., “Safety and Pharmacokinetics of PA-001, a New Potential COVID-19 Drug That Targets the S2 Subunit of SARS-CoV-2 Spike Protein, in Healthy Subjects,” Poster Abstracts; Abstract citation ID: ofad500.2…
[cited by applicant]
Kurhade C et al., Low neutralization of SARS-CoV-2 Omicron BA.2.75.2, BQ.1.1 and XBB.1 by parental mRNA vaccine or a BA.5 bivalent booster. Nat Med. Feb. 2023;29(2):344-347. Safety and efficacy of inhaled IBIO123 for se…
[cited by applicant]
Ladde, S.M. et al., “Safety and efficacy of inhaled IBIO123 for severe COVID-19: a randomised, double-blind, dose-ascending, placebo-controlled, phase 1/2 trial,” The Lancet, 35 pages (2023).
[cited by applicant]
Ladner, J. T., et al., “Epitope-resolved profiling of the SARS-CoV-2 antibody response identifies cross-reactivity with endemic human coronaviruses”, Cell Reports Medicine, vol. 2 No. 1, Jan. 1, 2021, 18 pages.
[cited by applicant]
Laracy JC et al., Long and persistent COVID-19 in patients with hematologic malignancies: from bench to bedside. Curr Opin Infect Dis. Aug. 1, 2022;35(4):271-279. doi: 10.1097/QCO.0000000000000841. Epub Jul. 5, 2022. PM…
[cited by applicant]
Leach, M.W. et al., “Use of tissue cross-reactivity studies in the development of antibody-based biopharmaceuticals: history, experience, methodology, and future directions,” Toxicol Pathol, vol. 38; No. 7; 1138-1166 (2…
[cited by applicant]
Levin EG et al., Waning Immune Humoral Response to BNT162b2 Covid-19 Vaccine over 6 Months. N Engl J Med. Dec. 9, 2021;385(24):e84. doi: 10.1056/NEJMoa2114583. Epub Oct. 6, 2021. PMID: 34614326; PMCID: PMC8522797.
[cited by applicant]
Levin M.J. et al., “Intramuscular AZD7442 (Tixagevimab-Cilgavimab) for Prevention of Covid-19,” N. Engl. J. Med., vol. 386; No. 23; 2188-2200 (2022).
[cited by applicant]
Levin M.J. et al., “Intramuscular AZD7442 (Tixagevimab-Cilgavimab) for Prevention of Covid-19,” N. Engl. J. Med., vol. 386; No. 23; 2188-2200; The Protocol; 424 pages (2022).
[cited by applicant]
Levin, M.J. et al., “AZD7442 (Tixagevimab/Cilgavimab) for Post-Exposure Prophylaxis of Symptomatic Coronavirus Disease 2019,” Clinical Infectious Diseases, vol. 76; No. 7; 1247-1256 (2023).
[cited by applicant]
Li W. et al., “Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern,” Cell Rep., vol. 38; No. 2; 110210; 28 pages (2022).
[cited by applicant]
Gubbins et al., “Molecular characterization of a panel of murine monoclonal antibodies specific for the SARS-coronavirus”, Molecular Immunology, vol. 42, No. 1, 2005, pp. 125-136.
[cited by applicant]