Important note: Information in this article was accurate in April 2001. The state of the art may have changed since the publication date.AIDSWEEKLY Plus; Monday, April 9, 2001
Michael Greer, Staff Medical Writer
NewsRx - The mechanisms by which the HIV antibody 17b interferes with viral cell entry may aid in the creation of new HIV inhibitors, say researchers in Pennsylvania.
"HIV 1 utilizes CD4 and the chemokine coreceptor for viral entry," I. Chaiken and colleagues explained in the journal Biochemistry. "The coreceptor CCR5 binding site on gp120 partially overlaps with the binding epitope of 17b, a neutralizing antibody of HIV 1."
After studying the kinetic interactions between HIV proteins and cellular binding sites, Chaiken et al. found that 17b may partially block the envelope protein gp120 from both the CCR5 and CD4 binding sites.
While normal gp120 showed reduced binding affinity in the presence of 17b, gp120 mutants lacking the V1/V2 loops did not (for the most part) suffer from this inhibition, they said.
Chaiken et al. suggested that these loops may get in the way of the CD4 binding site when 17b is prebound to "healthy" gp120, weakening interactions between gp120 and soluble CD4.
Reduced CD4 binding affinity for gp120 would then act as a second means of viral inhibition, in addition to partial blocking of the CCR5 binding site ("Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4," Biochemistry, 2001;40(6):1662-1670).
"This negative cooperative effect of 17b may provide insight into approaches to designing antagonists for viral entry," Chaiken and colleagues concluded.
The corresponding author for this report is I. Chaiken, 909 Stellar Change Labs, 422 Curie Boulevard, Philadelphia, PA 19104 USA.
Key points reported in this study include:
This article was prepared by AIDS Weekly editors from staff and other reports.
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