Abstract
APOBEC3G belongs to the family of cellular cytidine deaminase-editing enzymes with a potent antiretroviral activity, which is counteracted by the Vif protein expressed by lentiviruses. Antiretroviral activity of APOBEC3G requires its packaging into assembling virions, presumably to ensure its close association with nascent retroviral cDNA. Here, we demonstrate that APOBEC3G is encapsidated through a direct interaction with the HIV-1 Gag polyprotein which likely takes place on the membranes of the multivesicular bodies (MVB)/late endosomal compartments. This interaction is mediated by the Gag nucleocapsid protein NC, and the N-terminal part of NC is most critical for this interaction. Binding to the NC domain would ensure that APOBEC3G will be concentrated in the viral core of mature HIV-1, in close proximity to the reverse transcription complex.
Highlights
APOBEC3G belongs to the family of cellular cytidine deaminase-editing enzymes with a potent antiretroviral activity, which is counteracted by the Vif protein expressed by lentiviruses
Antiretroviral activity of APOBEC3G requires its encapsidation into assembling virions, presumably to ensure its close association with the retroviral reverse transcription complex and nascent retroviral cDNA
Since Gag itself is sufficient to drive the assembly of virus-like particles (VLPs), we reasoned that reduction of GFPAPOBEC3G expression in cells resulted from APOBEC3G packaging into VLPs, most likely through the interaction with Gag
Summary
APOBEC3G belongs to the family of cellular cytidine deaminase-editing enzymes with a potent antiretroviral activity, which is counteracted by the Vif protein expressed by lentiviruses. Printed in U.S.A. APOBEC3G Is Incorporated into Virus-like Particles by a Direct Interaction with HIV-1 Gag Nucleocapsid Protein*
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