Murine leukemia virus glycoGag antagonizes SERINC5 via ER-phagy receptor RETREG1.

ABSTRACT: Serine incorporator 5 (SERINC5) is a host restriction factor that inhibits the infectivity of certain enveloped viruses, including human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MLV), by incorporating into the viral envelope and blocking viral entry. To counteract this, HIV-1 and MLV encode accessory proteins-Nef and glycoGag, respectively-that downregulate SERINC5 expression in producer cells. Here, we demonstrate that glycoGag employs more complex and effective mechanisms than Nef to antagonize SERINC5. Despite being a type II integral membrane protein, glycoGag primarily localizes to the cytoplasm, while Nef is mainly associated with the plasma membrane. Additionally, glycoGag is rapidly degraded by proteasomes, in contrast to the greater stability of Nef, and be

SUBMITTER: Ahmad I 

PROVIDER: S-EPMC12530543 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature