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.
Antigens, CD4/*METABOLISM HIV Antigens/*GENETICS
HIV-1/*GENETICS/METABOLISM HIV-2/*GENETICS/METABOLISM *Mutation
ABSTRACT