Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly.

ABSTRACT: For most retroviruses, including HIV-1, binding of the Gag polyprotein to the plasma membrane (PM) is mediated by interactions between Gag's N-terminal myristoylated matrix (MA) domain and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂) in the PM. The Gag protein of avian sarcoma virus (ASV) lacks the N-myristoylation signal but contains structural domains having functions similar to those of HIV-1 Gag. The molecular mechanism by which ASV Gag binds to the PM is incompletely understood. Here, we employed NMR techniques to elucidate the molecular determinants of the membrane-binding domain of ASV MA (MA₈₇) to lipids and liposomes. We report that MA₈₇ binds to the polar head of phosphoinositides such as PI(4,5)P₂ We found that MA₈₇

SUBMITTER: Vlach J 

PROVIDER: S-EPMC6295720 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature