Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity.

摘要: Recent studies suggest that HIV-1 budding occurs selectively from detergent-insoluble membrane domains, referred to as lipid rafts. Palmitoylation is thought be one of the factors responsible for targeting proteins The cytoplasmic domain envelope glycoprotein (gp160) contains two palmitoylated cysteine residues. In this work, we studied solubility gp160 after detergent extraction. We show wild-type mostly insoluble ice-cold Triton X-100 extraction, but it becomes almost completely soluble at 37°C. contrast, find a mutant gp160, in which residues are replaced by serine, even under These findings consistent with properties localize rafts and strongly associated Further, removal both palmitoylation sites results formation virus low levels incorporation well decrease viral infectivity 60-fold. Our support suggestion buds point role assembly hub.