[HTML][HTML] Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif

R Mariani, D Chen, B Schröfelbauer, F Navarro… - Cell, 2003 - cell.com
R Mariani, D Chen, B Schröfelbauer, F Navarro, R König, B Bollman, C Münk…
Cell, 2003cell.com
The HIV-1 accessory protein Vif (virion infectivity factor) is required for the production of
infectious virions by CD4+ lymphocytes. Vif facilitates particle infectivity by blocking the
inhibitory activity of APOBEC3G (CEM15), a virion-encapsidated cellular protein that
deaminates minus-strand reverse transcript cytosines to uracils. We report that HIV-1 Vif
forms a complex with human APOBEC3G that prevents its virion encapsidation. HIV-1 Vif did
not efficiently form a complex with mouse APOBEC3G. Vif dramatically reduced the amount …
Abstract
The HIV-1 accessory protein Vif (virion infectivity factor) is required for the production of infectious virions by CD4+ lymphocytes. Vif facilitates particle infectivity by blocking the inhibitory activity of APOBEC3G (CEM15), a virion-encapsidated cellular protein that deaminates minus-strand reverse transcript cytosines to uracils. We report that HIV-1 Vif forms a complex with human APOBEC3G that prevents its virion encapsidation. HIV-1 Vif did not efficiently form a complex with mouse APOBEC3G. Vif dramatically reduced the amount of human APOBEC3G encapsidated in HIV-1 virions but did not prevent encapsidation of mouse or AGM APOBEC3G. As a result, these enzymes are potent inhibitors of wild-type HIV-1 replication. The species-specificity of this interaction may play a role in restricting HIV-1 infection to humans. Together these findings suggest that therapeutic intervention that either induced APOBEC3G or blocked its interaction with Vif could be clinically beneficial.
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