Abstract
The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161-164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 49-53 |
| Number of pages | 5 |
| Journal | Virology |
| Volume | 377 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 20 2008 |
Funding
We thank Lorraine Sutton for help with p24 assays and DNA sequencing, Megan Johnson for plasmid pA3G-HA and Chisu Song for careful reading and critical evaluation of this manuscript. This work was supported by a Vanderbilt-Meharry Center for AIDS Research (CFAR) Developmental grant (J.P.D.) and National Institutes of Health grants R21 AI068490 (J.P.D.) and RO1 AI29193 (RTD). This work has been facilitated by the infrastructure and resources provided by the Vanderbilt-Meharry CFAR, funded by NIH program P30 AI54999.
Keywords
- APOBEC3G
- HIV-1 Vif
- Vif PPLP motif
- Vif multimerization
ASJC Scopus subject areas
- Virology
