AIDSWEEKLY Plus; Monday, March 15, 2004
Staff Medical Writers

"The key role of gp120 in the cellular entry of HIV makes this glycoprotein an attractive target for new drugs," virologists in France explained. "Various polyanions bind to the positively charged V3 loop of gp120."

In a recent study, J. Dairou and colleagues at the University of Paris VI examined "a series of anionic porphyrins bearing two sulfonate groups and two carboxylic chains with various degree of esterification."

"These molecules carry an overall negative charge between 4 and 2," they wrote in the journal Antiviral Research. "Upon activation by light, these compounds, known as photosensitizers, produce highly reactive oxygen species able to damage amino acid chains. The interactions of these molecules with the V3 loop and a positively charged area in the C5 region were investigated in the dark by using specific antibodies and ELISA protocols."

"Competitive inhibition of the anti-V3 antibody was observed with an increased efficiency for the esterified compounds," published data indicated. "No evidence for binding to the C5 region was found."

"In contrast, when gp120 was irradiated with light in presence of the porphyrin prior to the addition of the antibody, strong inhibition of the anti-C5 antibody was observed revealing irreversible photo-damages in this region," test results showed. "No effect on the V3 loop was observed."

"Irradiations at two wavelengths made it possible to identify porphyrin monomers as the photoactive forms despite the presence of large excess of dimers in the incubation solution," according to the report.

"It is suggested that porphyrins bound to the V3 loop could produce photo-damages at some distance, in particular within the C5 region that contains several photosensitive amino acids," the researchers concluded.

Dairou and coauthors published the results of their study in Antiviral Research (Interaction of sulfonated anionic porphyrins with HIV glycoprotein gp120: photodamages revealed by inhibition of antibody binding to V3 and C5 domains. Antiviral Res. 2004 Jan;61(1):37-47.

For additional information, contact D. Brault, University of Paris VI, CNRS, UMR 7033, Laboratory of Biomolecular and Cellular Physicochemistry, F-75005 Paris, France.

The publisher of the journal Antiviral Research can be contacted at: Elsevier Science B.V., P.O. Box 211, 1000 AE Amsterdam, the Netherlands.

The information in this article comes under the major subject areas of AIDS & HIV, Biotechnology, Pharmaceutical & Drug Development, Proteomics and Virology.

This article was prepared by AIDS Weekly editors from staff and other reports. Copyright 2004, AIDS Weekly via NewsRx.com & NewsRx.net.

Reference

Dairou J, Vever-Bizet C, Brault D. "Interaction of sulfonated anionic porphyrins with HIV glycoprotein gp120: photodamages revealed by inhibition of antibody binding to V3 and C5 domains", Antiviral Res. 2004 Jan;61(1):37-47

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