A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction

Monir Ejemel(University of Massachusetts Chan Medical School), Qi Li(University of Massachusetts Chan Medical School), Shurong Hou(University of Massachusetts Chan Medical School), Zachary A. Schiller(University of Massachusetts Chan Medical School), Julia A. Tree(Public Health England), Aaron Wallace(University of Massachusetts Chan Medical School), Alla Amcheslavsky(University of Massachusetts Chan Medical School), Neşe Kurt Yılmaz(University of Massachusetts Chan Medical School), Karen R. Buttigieg(Public Health England), Michael J. Elmore(Public Health England), Kerry Godwin(Public Health England), Naomi S. Coombes(Public Health England), Jacqueline R. Toomey(University of Massachusetts Chan Medical School), Ryan M. Schneider(University of Massachusetts Chan Medical School), Anudeep S. Ramchetty(University of Massachusetts Chan Medical School), Brianna J. Close(Boston University), Da‐Yuan Chen(Boston University), Hasahn L. Conway(Boston University), Mohsan Saeed(Boston University), Chandrashekar Ganesa(University of Massachusetts Chan Medical School), Miles W. Carroll(Public Health England), Lisa A. Cavacini(University of Massachusetts Chan Medical School), Mark S. Klempner(University of Massachusetts Chan Medical School), Celia A. Schiffer(University of Massachusetts Chan Medical School), Yang Wang(University of Massachusetts Chan Medical School)
Nature Communications
August 21, 2020
10.1038/s41467-020-18058-8
Cited by 181Open Access
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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.

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