Abstract
The HIV-1 envelope protein is a glycoprotein composed of 120 kD and 41 kD subunits. It contains 30-38 potential asparagine-linked glycosylation sites which have been shown to play a role in CD4 binding, virus uptake, and cytopathogenicity. Several inhibitors of oligosaccharide attachment or modification have been tested. An agent which inhibits glucosidases, N-butyl deoxynojirimycin was found to inhibit HIV-1 and SIVmac infectivity, and is currently in clinical trials.
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