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Single point mutations in the HIV envelope gene encoding the extracellular glycoprotein affect viral tropism and receptor binding.


Int Conf AIDS. 1989 Jun 4-9;5:526 (abstract no. W.C.O.14). Unique

OBJECTIVE: To investigate the functional significance of the domains of the envelope protein that are highly conserved between HIV-1 and HIV-2. METHODS: Short deletions or point mutations were made within the highly conserved regions of the envelope gene and the mutated genes were expressed in vaccinia virus recombinants, plasmid vectors, and/or infectious HIV proviral clones. Receptor binding was analysed by co-immunoprecipitation with soluble CD4. Supernatants from transfection of proviral clones were assayed for infectivity. RESULTS: In vitro studies revealed that the integrity of at least four domains of the envelope protein was indispensable for binding to the receptor. Detailed studies of one of these regions demonstrates that a single amino acid change can be critical for binding to CD4 molecule in vitro. Mutation of another highly conserved amino acid in this region did not drastically affect receptor binding but surprisingly, the tropism of the virus particles containing this mutation was modified. CONCLUSION: Single amino acid changes in highly conserved regions of the envelope gene can have critical effects on receptor binding and cell tropism.



Information in this article was accurate in September 30, 1990. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.