Antibody-mediated cell entry of SARS-CoV-2
Kibria, M. G.; Lavine, C. L.; Tang, W.; Wang, S.; Gao, H.; Shi, W.; Zhu, H.; Voyer, J.; Rits-Volloch, S.; Keerti, F.; Bi, C.; Peng, H.; Wesemann, D.; Lu, J.; Xie, H.; Seaman, M. S.; Chen, B.
Show abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) enters host cells by first engaging its cellular receptor angiotensin converting enzyme 2 (ACE2) to induce conformational changes in the virus-encoded spike protein and fusion between the viral and target cell membranes. We report here that certain monoclonal neutralizing antibodies against distinct epitopic regions of the receptor-binding domain of the spike can replace ACE2 to serve as a receptor and efficiently support membrane fusion and viral infectivity. These receptor-like antibodies can function in the form of a complex of their soluble immunoglobulin G with Fc-gamma receptor I, a chimera of their antigen-binding fragment with the transmembrane domain of ACE2 or a membrane-bound B cell receptor, indicating that ACE2 and its specific interactions with the spike protein are dispensable for SARS-CoV-2 entry. These results suggest that antibody responses against SARS-CoV-2 may expand the viral tropism to otherwise nonpermissive cell types; they have important implications for viral transmission and pathogenesis.
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