US 3766162A
· Spector
· 1973
[cited by applicant]
US 3791932A
· Weemen et al.
· 1974
[cited by applicant]
US 3817837A
· Ullman et al.
· 1974
[cited by applicant]
US 4179337A
· Davis et al.
· 1979
[cited by applicant]
US 4233402A
· Maggio et al.
· 1980
[cited by applicant]
US 4495285A
· Shimizu et al.
· 1985
[cited by applicant]
US 4609546A
· Hiratani et al.
· 1986
[cited by applicant]
US 4676980A
· Segal et al.
· 1987
[cited by applicant]
US 4766106A
· Katre et al.
· 1988
[cited by applicant]
US 4831175A
· Gansow et al.
· 1989
[cited by applicant]
US 5595721A
· Kaminski et al.
· 1997
[cited by applicant]
US 5807715A
· Morrison et al.
· 1998
[cited by applicant]
US 6300064B1
· Knappik et al.
· 2001
[cited by applicant]
US 6300104B1
· Morrison et al.
· 2001
[cited by applicant]
US 8101553B1
· Kurosawa et al.
· 2012
[cited by applicant]
US 8871207B2
· Lanzavecchia et al.
· 2014
[cited by applicant]
US 9243054B2
· Burioni et al.
· 2016
[cited by applicant]
US 10294292B2
· Kallewaard-Lelay et al.
· 2019
[cited by applicant]
US 10442854B2
· Kallewaard-Lelay et al.
· 2019
[cited by applicant]
US 10519221B2
· Kallewaard-Lelay et al.
· 2019
[cited by applicant]
US 11174304B2
· Kallewaard-Lelay et al.
· 2021
[cited by applicant]
US 20070219149A1
· Hasegawa et al.
· 2007
[cited by applicant]
US 20120128684A1
· Marasco et al.
· 2012
[cited by applicant]
US 20190015509A1
· Kallewaard-Lelay et al.
· 2019
[cited by applicant]
CN 1671741A
· 2005
[cited by applicant]
EP 1167382A1
· 2002
[cited by applicant]
EP 2919813B1
· 2018
[cited by applicant]
RU 2536956C1
· 2014
[cited by applicant]
WO 0052031A2
· 2000
[cited by applicant]
WO 0052473A2
· 2000
[cited by applicant]
WO 2004007667A2
· 2004
[cited by applicant]
WO 2004001007A2
· 2004
[cited by applicant]
WO 2005007697A1
· 2005
[cited by applicant]
WO 2006124269A2
· 2006
[cited by applicant]
WO 2007045477A2
· 2007
[cited by applicant]
WO 2007109742A2
· 2007
[cited by applicant]
WO 2007117577A2
· 2007
[cited by applicant]
WO 2007134327A2
· 2007
[cited by applicant]
WO 2008028946A2
· 2008
[cited by applicant]
WO 2008054606A2
· 2008
[cited by applicant]
WO 2008066691A2
· 2008
[cited by applicant]
WO 2008076379A2
· 2008
[cited by applicant]
WO 2008084410A2
· 2008
[cited by applicant]
WO 2008110937A2
· 2008
[cited by applicant]
WO 2009115972A1
· 2009
[cited by applicant]
WO 2010010466A2
· 2010
[cited by applicant]
WO 2010010467A2
· 2010
[cited by applicant]
WO 2010054007A1
· 2010
[cited by applicant]
WO 2012082634A1
· 2012
[cited by applicant]
WO 2013007770A1
· 2013
[cited by applicant]
WO 2013011347A1
· 2013
[cited by applicant]
WO 2013043729A1
· 2013
[cited by applicant]
WO 2013044203A2
· 2013
[cited by applicant]
WO 2013086052A2
· 2013
[cited by applicant]
WO 2013132007A1
· 2013
[cited by applicant]
WO 2014078268A1
· 2014
[cited by applicant]
WO 2014158001A1
· 2014
[cited by applicant]
WO 2015051010A1
· 2015
[cited by applicant]
WO 2016011035A2
· 2016
[cited by applicant]
WO 2016196470A1
· 2016
[cited by applicant]
WO 2017123685A1
· 2017
[cited by applicant]
WO 2017147248A1
· 2017
[cited by applicant]
Dreyfus et al. Science. 14;337 (6100):13438 (Year: 2012).
[cited by examiner]
Davies and Riechmann. “Affinity improvement of single antibody VH domains: residues in all three hypervariable regions affect antigen binding.” Immunotechnology. 2:169-179 (1996).
[cited by applicant]
Holt et al. “Domain antibodies: proteins for therapy.” TRENDS Biotech. 21(11):484 (2003).
[cited by applicant]
Centers for Disease Control and Prevention (CDC), “Antiviral Drugs for Seasonal Influenza: Additional Links and Resources”, last reviewed Nov. 30, 2020, 2 pages.
[cited by applicant]
Deyde, Varough M. et al., “Surveillance of Resistance to Adamantanes among Influenza A(H3N1) Viruses Isolated Worldwide,” JID, 2007:196 (Jul. 15), pp. 249-257.
[cited by applicant]
Duwe, Susanne, “Influenza viruses—antiviral therapy and resistance,” GMS Infectious Diseases, 2017, vol. 5, pp. 1-10.
[cited by applicant]
Fan, Gaowei et al., “Bispecific antibodies and their applications,” Journal of Hematology &2015, 14 pages.
[cited by applicant]
Holliger, Philipp et al., “Diabodies: Small bivalent and bispecific antibody fragments,” Proc. Natl. Acad. Sci. USA, vol. 90, Jul. 1993, pp. 6444-6448.
[cited by applicant]
Lampejo, Temi, “Influenza and antiviral resistance: an overview”, European Journal of Clinical Microbiology & Infectious Diseases, Feb. 13, 2020, 8 pages.
[cited by applicant]
Abed et al., “A Review of Clinical Influenza A and B Infections with Reduced Susceptibility to Both Oseltamivir and Zanamivir,” Open Forum Infectious Diseases 4(3): ofx105 (2017).
[cited by applicant]
Ali et al., “Evaluation of MEDI8852, an Anti-Influenza A Monoclonal Antibody, in Treating Acute Uncomplicated Influenza,” Antimicrobial Agents and Chemotherapy 62(11): e00694-18 (2018).
[cited by applicant]
Pakula and Sauer, “Genetic Analysis of Protein Stability and Function.” Annu. Rev. Genet. 23:289-310 (1989).
[cited by applicant]
Pan et al., “Weight-based Dosing in Medication Use: What Should We Know?” Patient Preference and Adherence 10: 549-560 (2016).
[cited by applicant]
Office Action in Chinese Application No. 201580038244.1 issued Jan. 17, 2020.
[cited by applicant]
Office Action in Japanese Application No. 2017-561892 issued Jun. 2, 2020.
[cited by applicant]
Non-final Office Action in U.S. Appl. No. 16/560,040 issued Apr. 16, 2020.
[cited by applicant]
Office Action in U.S. Appl. No. 16/068,941 issued Feb. 5, 2020.
[cited by applicant]
Bouvier, “The Future of Influenza Vaccines: A Historical and Clinical Perspective,” Vaccines 6:58 (2018).
[cited by applicant]
Deyev et al., “Modern Technologies for Creating Synthetic Antibodies for Clinical Application,” Acta Naturae, 1. 32-50 (2009).
[cited by applicant]
GENBANK Accession ID AAK94805.1, immunoglobulin light chain variable region, partial [
[cited by applicant]
GENBANK Accession ID ACS95408.1, immunoglobulin heavy chain variable region, partial [
[cited by applicant]
Ignatiev et al., Peculiarities of the Antigenic Structure of Hemagglutinin, Recognizable by Antibodies against Modern Viruses of Influenza A Subtypes H5 and H1 (2012).
[cited by applicant]
Kallewaard et al., “Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes,” Cell 166: 596-608 (2016).
[cited by applicant]
Lin et al., “Recent Changes Among Human Influenza Viruses,” Virus Res., 103: 47-52 (2004).
[cited by applicant]
Roit et al. Immunology [Textbook source], p. 49 (1991).
[cited by applicant]
Office Action in U.S. Appl. No. 15/026,276, issued Apr. 17, 2019.
[cited by applicant]
Office Action in U.S. Appl. No. 16/068,941, issued Oct. 21, 2019.
[cited by applicant]
Benjamin et al., “A Broadly Neutralizing Human Monoclonal Antibody Directed against a Novel Conserved Epitope on the Influenza Virus H3 Hemagglutinin Globular Head,” J Virol 88(12):6743-6750 (2014).
[cited by applicant]
Biere et al., “Differentiation of Influenza B Virus Lineages Yamagata and Victoria by Real-Time PCR,” J Clin Microbiol 48:1425-1427 (2010).
[cited by applicant]
Chai et al., “A broadly protective therapeutic antibody against influenza B virus with two mechanisms of action,” Nature Comm 8:14234 (2017).
[cited by applicant]
Corti et al., “Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine,” J Clin Invest 120:1663-1673 (2010).
[cited by applicant]
Corti et al., “A Neutralizing Antibody Selected from Plasma Cells That Binds to Group 1 and Group 2 Influenza A Hemagglutinins,” Science 333(6044):850-856 (2011).
[cited by applicant]
Corti et al., “Cross-neutralization of four paramyxoviruses by a human monoclonal antibody,” Nature 501 (7467):439-443 (2013).
[cited by applicant]
Corti et al., “Tackling influenza with broadly neutralizing antibodies,” Curr Opin Virol 24:60-69 (2017).
[cited by applicant]
Dreyfus et al., “Highly Conserved Protective Epitopes on Influenza B Viruses,” Science 337(6100):1343-1348 (2012).
[cited by applicant]
Ekiert et al., “Antibody recognition of a highly conserved influenza virus epitope: implications for universal prevention and therapy,” Science 324(5924):246-251 (2009).
[cited by applicant]
Ekiert et al., “A Highly Conserved Neutralizing Epitope on Group 2 Influenza A Viruses,” Science 333(6044):843-850 (2011).
[cited by applicant]
Ekiert et al., “Cross-neutralization of influenza A viruses mediated by a single antibody loop,” Nature 489 (7417):526-532 (2012).
[cited by applicant]
Friesen et al., “A common solution to group 2 influenza virus neutralization,” Proc Natl Acad Sci USA 111(1):445-450 (2014).
[cited by applicant]
Gerhard et al., “Prospects for Universal Influenza Virus Vaccine,” Emerg Infect Dis 12(4):569-574 (2006).
[cited by applicant]
Gioia et al., “Cross-subtype Immunity against Avian Influenza in Persons Recently Vaccinated for Influenza,” Emerg Infect Dis 14(1):121-128 (2008).
[cited by applicant]
Greenspan et al., “Defining epitopes: It's not as easy as it seems,” Nature Biotechnol 17:936-937 (1999).
[cited by applicant]
Hassantoufighi et al., “A practical influenza neutralization assay to simultaneously quantify hemagglutinin and neuraminidase-inhibiting antibody responses,” Vaccine 28:790-797 (2010).
[cited by applicant]
Kashyap et al., “Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies,” Proc Natl Acad Sci USA 105(16):5986-5991 (2008).
[cited by applicant]
Kaverin et al., “Epitope Mapping of the Hemagglutinin Molecule of a Highly Pathogenic H5N1 Influenza Virus by Using Monoclonal Antibodies,” J Virol 81(23):12911-12917 (2007).
[cited by applicant]
Kozbor et al., “The production of monoclonal antibodies from human lymphocytes,” Immunol Today 4(3):72-79 (1983).
[cited by applicant]
Krause et al., “A Broadly Neutralizing Human Monoclonal Antibody That Recognizes a Conserved, Novel Epitope on the Globular Head of the Influenza H1N1 Virus Hemagglutinin,” J Virol 85(20):10905-10908 (2011).
[cited by applicant]
Lee et al., “Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity,” Proc Natl Acad Sci USA 109(42):17040-17045 (2012).
[cited by applicant]
Li et al., “Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells,” Proc Natl Acad Sci USA 109(23):9047-9052 (2012).
[cited by applicant]
Nakamura et al., “An In Vivo Human-Plasmablast Enrichment Technique Allows Rapid Identification of Therapeutic Influenza A Antibodies,” Cell Host Microbe 14:93-103 (2013).
[cited by applicant]
Nguyen et al., “Heterosubtypic Immunity to Influenza A Virus Infection Requires B Cells but Not CD8+ Cytotoxic T Lymphocytes,” J Virol 183:368-376 (2001).
[cited by applicant]
Okuno et al., “A Common Neutralizing Epitope Conserved between the Hemagglutinins of Influenza A Virus H1 and H2 Strains,” J Virol 67(5):2552-2558 (1993).
[cited by applicant]
Pappas et al., “Rapid development of broadly influenza neutralizing antibodies through redundant mutations,” Nature 516(7531):418-422 (2014).
[cited by applicant]
Paul et al., eds. Fundamental Immunology 3rd Edition (1993), pp. 292-295.
[cited by applicant]
Prabhu et al., “Monoclonal Antibodies against the Fusion Peptide of Hemagglutinin Protect Mice from Lethal Influenza A Virus H5N1 Infection,” J Virol 83(6):2553-2562 (2009).
[cited by applicant]
Ren et al., “Epitope-focused vaccine design against influenza A and B viruses,” Curr Opin Immunol 42:83-90 (2016).
[cited by applicant]
Rowe et al., “Detection of Antibody to Avian Influenza A (H5N1) Virus in Human Serum by Using a Combination of Serologic Assays,” J Clin Microbiol 37(4):937-943 (1999).
[cited by applicant]
Rudikoff et al., “Single amino acid substitution altering antigen-binding specificity,” Proc Natl Acad Sci USA 79 (6):1979-1983 (1982).
[cited by applicant]
Simmons et al., “Prophylactic and Therapeutic Efficacy of Human Monoclonal Antibodies against H5N1 Influenza,” PLOS Med 4(5):e178 (2007).
[cited by applicant]
Smirnov et al., “Prevention and treatment of bronchopneumonia in mice caused by mouse-adapted variant of avian H5N2 influenza A virus using monoclonal antibody against conserved epitope in the HA stem region,” Arch Viro…
[cited by applicant]
Sui et al., “Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses,” Nature Struct Mol Biol 16(3):265-273 (2009).
[cited by applicant]
Temperton et al., “Longitudinally Profiling Neutralizing Antibody Response to SARS Coronavirus with Pseudotypes,” Emerg Infect Dis 11(3):411-416 (2005).
[cited by applicant]
Thompson et al., “Influenza-Associated Hospitalizations in the United States,” JAMA 292:1333-1340 (2004).
[cited by applicant]
Throsby et al., “Heterosubtypic Neutralizing Monoclonal Antibodies Cross-Protective against H5N1 and H1N1 Recovered from Human IgM+ Memory B Cells,” PLOS One 3(12):e3942 (2008).
[cited by applicant]
Traggiai et al., “An efficient method to make human monoclonal antibodies from memory B cells: potent neutralization of SARS coronavirus,” Nature Med 10:871-875 (2004).
[cited by applicant]
Vareckova et al., “HA2-specific monoclonal antibodies as tools for differential recognition of influenza A virus antigenic subtypes,” Virus Res 132(1-2):181-186 (2008).
[cited by applicant]
Wagner et al., “Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza activity,” Proc Natl Acad Sci USA 111(47):16820-16825 (2014).
[cited by applicant]
Wang, Qinghua et al., “Crystal Structure of Unliganded Influenza B Virus Hemagglutinin,” J Virol 82(6):3011-3020 (2008).
[cited by applicant]
Wang, Taia T. et al., “Broadly Protective Monoclonal Antibodies against H3 Influenza Viruses following Sequential Immunization with Different Hemagglutinins,” PLOS Pathog 6(2):e1000796 (2010).
[cited by applicant]
Whittle et al., “Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin,” Proc Natl Acad Sci USA 108(34):14216-14221 (2011).
[cited by applicant]
Wilson et al., “Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution,” Nature 289:366-373 (1981).
[cited by applicant]
Wrammert et al., “Rapid Cloning of High Affinity Human Monoclonal Antibodies Against Influenza Virus,” Nature 453 (7195):667-671 (2008).
[cited by applicant]
Wrammert et al., “Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection,” J Exp Med 208(1):181-193 (2011).
[cited by applicant]
Xiang et al., “Framework Residues 71 and 93 of the Chimeric B72.3 Antibody are Major Determinants of the Conformation of Heavy-chain Hypervariable Loops,” J Mol Biol 253:385-390 (1995).
[cited by applicant]
Yasugi et al., “Human Monoclonal Antibodies Broadly Neutralizing against Influenza B Virus,” PLOS Pathog 9(2): e1003150 (2013).
[cited by applicant]
Yoshida et al., “Cross-Protective Potential of a Novel Monoclonal Antibody Directed against Antigenic Site B of the Hemagglutinin of Influenza A Viruses,” PLOS Pathog 5(3):e1000350 (2009).
[cited by applicant]
Zabetakis et al., “Contributions of the Complementarity Determining Regions to the Thermal Stability of a Single-Domain Antibody,” PLoS One 8(10):e77678 (2013).
[cited by applicant]
Zhou et al., “Hospitalizations Associated With Influenza and Respiratory Syncytial Virus in the United States, 1993-2008,” Clin Infect Dis 54(10):1427-1436.
[cited by applicant]
Non-final Office Action issued in U.S. Appl. No. 15/026,276, dated Apr. 6, 2018.
[cited by applicant]
Non-final Office Action issued in U.S. Appl. No. 15/026,276, dated Oct. 19, 2018.
[cited by applicant]
Non-final Office Action issued in U.S. Appl. No. 15/325,603, dated Jun. 27, 2017.
[cited by applicant]
Final Office Action issued in U.S. Appl. No. 15/325,603, dated Mar. 8, 2018.
[cited by applicant]
Non-final Office Action issued in U.S. Appl. No. 15/325,603, dated Sep. 7, 2018.
[cited by applicant]
Non-final Office Action issued in U.S. Appl. No. 15/577,799, dated Feb. 21, 2019.
[cited by applicant]