The matrix domain of the Gag protein from avian sarcoma virus contains a PI(4,5)P₂-binding site that targets Gag to the cell periphery.

ABSTRACT: The Gag protein of avian sarcoma virus (ASV) lacks an N-myristoyl (myr) group, but contains structural domains similar to those of HIV-1 Gag. Similarly to HIV-1, ASV Gag accumulates on the plasma membrane (PM) before egress; however, it is unclear whether the phospholipid PI(4,5)P₂ binds directly to the matrix (MA) domain of ASV Gag, as is the case for HIV-1 Gag. Moreover, the role of PI(4,5)P₂ in ASV Gag localization and budding has been controversial. Here, we report that substitution of residues that define the PI(4,5)P₂-binding site in the ASV MA domain (reported in an accompanying paper) interfere with Gag localization to the cell periphery and inhibit the production of virus-like particles (VLPs). We show that co-expression of Sprouty2 (Spry2)

SUBMITTER: Watanabe SM 

PROVIDER: S-EPMC6295721 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature