Journal article

Efficacy of fusion peptide homologs in blocking cell lysis and HIV-induced fusion

KA Silburn, DA McPhee, AL Maerz, P Poumbourios, RG Whittaker, A Kirkpatrick, WG Reilly, MK Manthey, CC Curtain

AIDS RESEARCH AND HUMAN RETROVIRUSES | MARY ANN LIEBERT INC PUBL | Published : 1998

Abstract

Contrary to earlier reports, we have found that tri- and hexapeptides analogous or homologous with segments of the 23-residue N-terminal fusion sequence (FS) of the viral transmembrane glycoprotein gp41 (residues 517-539) did not significantly inhibit HIV-1-induced syncytium formation, using an uninfected cell-infected cell fusion assay. In contrast, we found that the high molecular weight apolipoprotein A-1 and a 23-residue analog of the FS, with the phenylalanine residues at positions 524 and 527 replaced with alanine residues, were effective inhibitors. Although the tripeptides were ineffective as inhibitors of syncytium formation, we found a number of them inhibited red cell lysis induce..

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University of Melbourne Researchers