In this report, we describe a crucial role of lipid raft-colocalized receptors in the entry of human immunodeficiency virus type 1 (HIV-1) into CD4 ؉ T cells. We show that biochemically isolated detergent-resistant fractions have characteristics of lipid rafts. Lipid raft integrity was required for productive HIV-1 entry as determined by (

No 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 Nterminal 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.