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.
| Original language | English |
|---|---|
| Pages (from-to) | 165-173 |
| Number of pages | 9 |
| Journal | AIDS research and human retroviruses |
| Volume | 8 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1992 |