In computer explore The neutralization mechanism of Amubarvimab and Romlusevimab against SARS-COV-2 mutants

Since the end of 2019, the coronavirus disease 2019 (COVID-19) has been endemic worldwide for three years, causing more than 6.95 million deaths and having a massive impact on the global political economy. With time, the Severe acute respiratory syndrome coronavirus 2 (SARS-COV-2) is also constantly mutating. Mutations lead to stronger infectivity or virulence of the virus, and some monoclonal antibodies against wild-type SARS-COV-2 are also challenging to play a role. Amubarvimab and Romlusevimab were originally developed against wild-type SARS-COV-2; however, these monoclonal antibodies' neutralizing efficacy and mechanism against these mutants are unknown. In this study, the binding ability of Amubarvimab and Romlusevimab to 7 mutant strains were tested by computer method and the interaction mechanism was explored. Our experimental data show that Amubarvimab can effectively bind most mutations and maintain the stability of the complexes mainly through hydrogen bond interaction; However, the binding efficiency of Romlusevimab was lower than that of Amubarvimab, and the stability of 18 the complexes was maintained mainly through electrostatic interaction. Both Amubarvimab and Romlusevimab show low binding potency against E406W and Q498Y mutations, so there is a certain probability of immune escape in the face of variants carrying E406W and Q498Y mutations when Amubarvimab and Romlusevimab are used in combination.