In silico tracking of SARS-CoV-2 Nsp1 structural variants in
SARS-CoV-2 non-structural protein 1 (Nsp1) is a virulence factor that
inhibits the innate immune response and translation of host mRNAs.
Despite the relevance of Nsp1, few studies have been conducted to
understand the effect of mutations on Nsp1 structure and function. Here,
we provide a molecular dynamics simulation of SARS-CoV-2 and SARS-CoV-1
Nsp1 conformational changes. Our data supports the idea that SARS-CoV-2
Nsp1 has a less compact structure than SARS-CoV-1 Nsp1. Moreover,
several mutations in the helix-loop-helix motif of Nsp1 C-terminal that
may affect the interactions of the Nsp1-ribosome complex were
investigated. Disordered regions in Nsp1 probably affect host-virus
interactions, cross-species transmission, and virus-host range. Overall,
these findings reinforce the importance of studying Nsp1 conformational
changes in new variants and its effect on virulence of SARS-CoV-2, by
altering inhibition potency of host mRNA translation efficiency.