Intricacies of the SARS-CoV-2 spike transmembrane trimer organization

Abstract

The spike glycoprotein (SGP) of SARS-CoV-2 effectuates membrane fusion and virus entry into target cells. A transmembrane domain (TMD) represents a homotrimer of alpha helices anchoring SGP in the viral envelope. Although SGP models available to date include TMD, its precise configuration was given brief consideration. Understanding viral fusion entails realistic TMD models, while no reliable approaches towards predicting the 3D structure of transmembrane homotrimers exist. Here, we adopted diverse computational tools to model the SGP TMD based solely on its primary structure.