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Abstract
The major challenge for the development of a highly effective peptide-based vaccine is represented by the diversity of HIV-1 strains among human population. HIV-1 matrix protein p17 is a candidate antigen for therapeutic vaccines against AIDS. Here we show that antibodies elicited in animals by immunizing them with a synthetic peptide representative of the p17 functional epitope (AT20) derived from HIV-1 BH10 (clade B), neutralize the biological activity of p17 derived from divergent strains displaying critical mutations within AT20, by recognizing a highly conserved conformational epitope. This finding shows that AT20, as an immunogenic molecule, elicits broadly neutralizing anti-p17 antibodies.
Published Version
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