Solution conformation of an immunogenic peptide derived from the principal neutralizing determinant of the HIV-2 envelope glycoprotein gp125.

Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

Solution conformation of an immunogenic peptide derived from the principal neutralizing determinant of the HIV-2 envelope glycoprotein gp125.

Fold Des. 1996;1(2):157-65. Unique Identifier : AIDSLINE MED/97233153
Campbell AP; Sykes BD; Norrby E; Assa-Munt N; Dyson HJ; Department of Molecular Biology, Scripps Research Institute, La Jolla,; California 92037, USA.

Abstract: BACKGROUND: The conformational preferences of a number of peptides with sequences related to the envelope glycoproteins of HIV-1 have been investigated in the past few years. Similar studies have not been made for HIV-2, which is a distinct virus with similar physiological effects to those of HIV-1. The discovery of common structural features would be a promising route to the design of immunogens for generally effective HIV vaccines. We present the results of an NMR conformational study of a sequence deriving from the V3 loop of HIV-2. RESULTS: Three synthetic immunogenic peptides were studied, of 12, 22 and 39 amino acids in length, all containing a central Met-Ser-Gly-Arg sequence conserved among a number of HIV-2 isolates. In addition, the 39-mer contained a disulfide bond between cysteine residues close to the ends of the molecule, forming a loop that is thought to comprise an important structural and immunological component of the intact glycoprotein. All three peptides display well defined beta-turns in the Met-Ser-Gly-Arg sequence, independent of the integrity of the disulfide bond. No other conformational preferences for folded conformations were found for the peptides. CONCLUSIONS: The presence of a beta-turn in the Met-Ser-Gly-Arg sequence is strikingly similar to the behavior seen for the corresponding principal neutralizing determinant sequence from gp120 of HIV-1 and argues, in the absence of information of the three-dimensional structure of the intact proteins, for a similarity in the structure of this region that could be exploited in the design of synthetic peptide vaccines generally effective against HIV infections.

Keywords: *Gene Products, env/CHEMISTRY *Gene Products, env/IMMUNOLOGY *HIV Antigens/CHEMISTRY *HIV-2/CHEMISTRY *HIV-2/IMMUNOLOGY *Peptides/CHEMISTRY *Peptides/IMMUNOLOGY *Protein Precursors/CHEMISTRY *Protein Precursors/IMMUNOLOGY
970730
M9772103

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