HIV relies on neddylation for ubiquitin ligase-mediated functions.

ABSTRACT:

Background

HIV and SIV defeat antiviral proteins by usurping Cullin-RING E3 ubiquitin ligases (CRLs) and likely influence other cellular processes through these as well. HIV-2 viral protein X (Vpx) engages the cullin4-containing CRL4 complex to deplete the antiviral protein SAMHD1. Vif expressed by HIV-1 and HIV-2 taps a cullin5 ubiquitin ligase complex to mark the antiviral protein APOBEC3G for destruction. Viral Protein R of HIV-1 (Vpr) assembles with the CRL4 ubiquitin ligase complex to deplete uracil-N-glycosylase2 (UNG2). Covalent attachment of the ubiquitin-like protein side-chain NEDD8 functionally activates cullins which are common to all of these processes.

Results

The requirement for neddylation in HIV-1 and HIV-2 infectivity was tested in the presence of APOBEC3G

SUBMITTER: Nekorchuk MD 

PROVIDER: S-EPMC3842660 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature