501Y.V2 spike protein resists the neutralizing antibody in atomistic simulations.

ABSTRACT: SARS-CoV-2 outbreaks worldwide caused COVID-19 pandemic, which is related to several million deaths. In particular, SARS-CoV-2 Spike (S) protein is a major biological target for COVID-19 vaccine design. Unfortunately, recent reports indicated that Spike (S) protein mutations can lead to antibody resistance. However, understanding the process is limited, especially at the atomic scale. The structural change of S protein and neutralizing antibody fragment (FAb) complexes was thus probed using molecular dynamics (MD) simulations. In particular, the backbone RMSD of the 501Y.V2 complex was significantly larger than that of the wild-type one implying a large structural change of the mutation system. Moreover, the mean of R_g, CCS, and SASA are almost the same when compared two complex

SUBMITTER: Ngo ST 

PROVIDER: S-EPMC8769535 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature