Investigating SARS-CoV-2 ORF7a and BST-2 heterodimerization by molecular dynamics simulations

Abstract

ORF7a, a single-pass transmembrane protein, localizes to the endoplasmic reticulum-Golgi intermediate compartment. Its interaction with BST-2 associates to suppress host immune response against the virulence of SARS-CoV-2; however, a structural model of protein-protein interface within the heterodimer is unknown. This work aims to investigate the ORF7a heterodimerization with the wild-type (WT) and a naturally-occurring single-point mutation BST-2 through molecular dynamics (MD) and provide insights into molecular interactions to understand the effect of a naturally BST-2 mutation.