An influenza HA stalk reactive polymeric IgA antibody exhibits anti-viral function regulated by binary interaction between HA and the antibody - Sano, Kaori; Saito, Shinji; Suzuki, Tadaki; Kotani, Osamu; Ainai, Akira; van Riet, Elly; Tabata, Koshiro; Saito, Kumpei; Takahashi, Yoshimasa; Yokoyama, Masaru; Sato, Hironori; Maruno, Takahiro; et al. (PloS one, 2021)
Keywords: Animals; Antibodies; Antibodies, Viral - chemistry; Antibodies, Viral - immunology; Antibody Affinity; Antiviral agents; Antiviral drugs; Binding sites; Binding Sites, Antibody; Biology and Life Sciences; Biotechnology; Cells, Cultured; Cloning; Dogs; Engineering schools; Fab; Female; Genomics; Glycan; Health aspects; HEK293 Cells; Hemagglutination inhibition; Hemagglutinins; Hemagglutinins - chemistry; Hemagglutinins - immunology; Humans; Immunogenicity, Vaccine; Immunoglobulin A; Immunoglobulin A - chemistry; Immunoglobulin A - immunology; Immunoglobulin G; Infections; Infectious diseases; Influenza; Influenza A Virus, H5N1 Subtype - immunology; Influenza Vaccines - immunology; Influenza, Human - prevention & control; Madin Darby Canine Kidney Cells; Medicine and Health Sciences; Mice; Mice, Inbred BALB C; Mucosa; Neutralization; Pathogens; Pathology; Physical Sciences; Polymerization; Polymers; Prevention; Properties (attributes); Research and Analysis Methods; Testing; Vaccines; Viruses; Japan