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Abstract
COVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity, or as a therapeutic, has yet been developed to SARS-CoV-2. In this study, we discover and characterize a cross-reactive human IgA monoclonal antibody, MAb362. MAb362 binds to both SARS-CoV and SARS-CoV-2 spike proteins and competitively blocks ACE2 receptor binding, by overlapping the ACE2 structural binding epitope. Furthermore, MAb362 IgA neutralizes both pseudotyped SARS-CoV and SARS-CoV-2 in 293 cells expressing ACE2. When converted to secretory IgA, MAb326 also neutralizes authentic SARS-CoV-2 virus while the IgG isotype shows no neutralization. Our results suggest that SARS-CoV-2 specific IgA antibodies, such as MAb362, may provide effective immunity against SARS-CoV-2 by inducing mucosal immunity within the respiratory system, a potentially critical feature of an effective vaccine.
Here, Ejemel et al. report the identification and characterization of a cross-neutralizing human IgA monoclonal antibody, named MAb362, that binds the receptor-binding domain of SARS-CoV-2 Spike, blocking its interaction with the ACE2 host receptor.
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1 MassBiologics of the University of Massachusetts Medical School, Boston, USA (GRID:grid.168645.8) (ISNI:0000 0001 0742 0364)
2 University of Massachusetts Medical School, Biochemistry and Molecular Pharmacology, Boston, USA (GRID:grid.168645.8) (ISNI:0000 0001 0742 0364)
3 Public Health England, Porton Down, National Infection Service, Salisbury, UK (GRID:grid.271308.f) (ISNI:0000 0004 5909 016X)
4 Boston University, National Emerging Infectious Diseases Laboratories, Boston, USA (GRID:grid.189504.1) (ISNI:0000 0004 1936 7558)