Stability and expression of SARS-CoV-2 spike-protein mutations.

ABSTRACT: Protein fold stability likely plays a role in SARS-CoV-2 S-protein evolution, together with ACE2 binding and antibody evasion. While few thermodynamic stability data are available for S-protein mutants, many systematic experimental data exist for their expression. In this paper, we explore whether such expression levels relate to the thermodynamic stability of the mutants. We studied mutation-induced SARS-CoV-2 S-protein fold stability, as computed by three very distinct methods and eight different protein structures to account for method- and structure-dependencies. For all methods and structures used (24 comparisons), computed stability changes correlate significantly (99% confidence level) with experimental yeast expression from the literature, such that higher expression is associated

SUBMITTER: Bæk KT 

PROVIDER: S-EPMC9612610 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature