Glycobiology, Vol 8, 131-137, Copyright © 1998 by Society for Glycobiology
HA Harrop and CC Rider
We have employed a direct radiolabel binding assay to investigate the
interaction between3H-heparin and recombinant envelope glycoproteins,
rgp120s, derived from several different isolates of HIV-1. Comparable
dose-dependent binding is exhibited by rgp120s from isolates IIIB, GB8, MN
and SF-2. Under identical experimental conditions the binding of3H- heparin
to a recombinant soluble form of the cellular receptor for gp120, CD4, is
negligible. The binding of3H-heparin to rgp120 is competed for by excess
unlabeled heparin and certain other, but not all, glycosaminoglycan and
chemically modified heparins. Of a range of such polysaccharides tested,
ability to compete with3H-heparin for binding was strictly correlated with
inhibition of HIV-1 replication in vitro. Those possessing potent
anti-HIV-1 activity were effective competitors, whereas those having no or
little anti-HIV-1 activity were poor competitors. Scatchard analysis
indicates that the K d of the interaction between heparin and rgp120 is 10
nM. Binding studies conducted in increasing salt concentrations confirm
that the interaction is ionic in nature. Synthetic 33-35 amino acid
peptides based on the sequence of the V3 loop of gp120 also bind to heparin
with high affinity. V3 loop peptides that are cyclized due to terminal
cysteine residues show more selective binding than their uncyclized
counterparts. Overall, these data demonstrate further that heparin exerts
its anti-HIV-1 activity by binding to the envelope glycoprotein of HIV-1,
rather than its cellular receptor, CD4. This study confirms that the V3
loop of gp120 is the site at which heparin exerts its anti- HIV-1 activity.
Moreover, it reveals that high affinity binding to heparin is shared by all
four rgp120s examined, despite amino acid substitutions within the V3 loop.
ORIGINAL ARTICLES
Heparin and its derivatives bind to HIV-1 recombinant envelope glycoproteins, rather than to recombinant HIV-1 receptor, CD4
Division of Biochemistry, Royal Holloway University of London, Surrey, UK.
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