Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoprotein.

ABSTRACT: The glycoproteins of hepatitis C virus, E1E2, are unlike any other viral fusion machinery yet described, and are the current focus of immunogen design in HCV vaccine development; thus, making E1E2 both scientifically and medically important. We used pre-existing, but fragmentary, structures to model a complete ectodomain of the major glycoprotein E2 from three strains of HCV. We then performed molecular dynamic simulations to explore the conformational landscape of E2, revealing a number of important features. Despite high sequence divergence, and subtle differences in the models, E2 from different strains behave similarly, possessing a stable core flanked by highly flexible regions, some of which perform essential functions such as receptor binding. Comparison with sequence data suggest t

SUBMITTER: Stejskal L 

PROVIDER: S-EPMC7065822 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature