OPEN bioRxiv : the preprint server for biology | 4 Aug 2020
Y Weisblum, F Schmidt, F Zhang, J DaSilva, D Poston, JCC Lorenzi, F Muecksch, M Rutkowska, HH Hoffmann, E Michailidis, C Gaebler, M Agudelo, A Cho, Z Wang, A Gazumyan, M Cipolla, L Luchsinger, CD Hillyer, M Caskey, DF Robbiani, CM Rice, MC Nussenzweig, T Hatziioannou and PD Bieniasz
Neutralizing antibodies elicited by prior infection or vaccination are likely to be key for future protection of individuals and populations against SARS-CoV-2. Moreover, passively administered antibodies are among the most promising therapeutic and prophylactic anti-SARS-CoV-2 agents. However, the degree to which SARS-CoV-2 will adapt to evade neutralizing antibodies is unclear. Using a recombinant chimeric VSV/SARS-CoV-2 reporter virus, we show that functional SARS-CoV-2 S protein variants with mutations in the receptor binding domain (RBD) and N-terminal domain that confer resistance to monoclonal antibodies or convalescent plasma can be readily selected. Notably, SARS-CoV-2 S variants that resist commonly elicited neutralizing antibodies are now present at low frequencies in circulating SARS-CoV-2 populations. Finally, the emergence of antibody-resistant SARS-CoV-2 variants that might limit the therapeutic usefulness of monoclonal antibodies can be mitigated by the use of antibody combinations that target distinct neutralizing epitopes.
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