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Title: Determination of the minimal fusion peptide of bovine leukemia virus gp30

Abstract

In this study, we determined the minimal N-terminal fusion peptide of the gp30 of the bovine leukemia virus on the basis of the tilted peptide theory. We first used molecular modelling to predict that the gp30 minimal fusion peptide corresponds to the 15 first residues. Liposome lipid-mixing and leakage assays confirmed that the 15-residue long peptide induces fusion in vitro and that it is the shortest peptide inducing optimal fusion since longer peptides destabilize liposomes to the same extent but not shorter ones. The 15-residue long peptide can thus be considered as the minimal fusion peptide. The effect of mutations reported in the literature was also investigated. Interestingly, mutations related to glycoproteins unable to induce syncytia in cell-cell fusion assays correspond to peptides predicted as non-tilted. The relationship between obliquity and fusogenicity was also confirmed in vitro for one tilted and one non-tilted mutant peptide.

Authors:
 [1];  [1];  [2];  [3];  [1]
  1. Centre de Biophysique Moleculaire Numerique, Faculte Universitaire des Sciences Agronomiques, 2 Passage des deportes, B-5030 Gembloux (Belgium)
  2. Ludwig Institute for Cancer Research-Brussels Branch, 74 Avenue Hippocrate, B-1200 Brussels (Belgium)
  3. Centre de Biophysique Moleculaire Numerique, Faculte Universitaire des Sciences Agronomiques, 2 Passage des deportes, B-5030 Gembloux (Belgium). E-mail: brasseur.r@fsagx.ac.be
Publication Date:
OSTI Identifier:
20979875
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2007.01.182; PII: S0006-291X(07)00258-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ABSORPTION SPECTROSCOPY; AIDS VIRUS; CATTLE; CELL MEMBRANES; FOURIER TRANSFORMATION; GLYCOPROTEINS; IN VITRO; INFRARED SPECTRA; LEUKEMIA VIRUSES; LIPIDS; LIPOSOMES; MUTANTS; MUTATIONS; PEPTIDES; SIMULATION

Citation Formats

Lorin, Aurelien, Lins, Laurence, Stroobant, Vincent, Brasseur, Robert, and Charloteaux, Benoit. Determination of the minimal fusion peptide of bovine leukemia virus gp30. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.01.182.
Lorin, Aurelien, Lins, Laurence, Stroobant, Vincent, Brasseur, Robert, & Charloteaux, Benoit. Determination of the minimal fusion peptide of bovine leukemia virus gp30. United States. doi:10.1016/j.bbrc.2007.01.182.
Lorin, Aurelien, Lins, Laurence, Stroobant, Vincent, Brasseur, Robert, and Charloteaux, Benoit. Fri . "Determination of the minimal fusion peptide of bovine leukemia virus gp30". United States. doi:10.1016/j.bbrc.2007.01.182.
@article{osti_20979875,
title = {Determination of the minimal fusion peptide of bovine leukemia virus gp30},
author = {Lorin, Aurelien and Lins, Laurence and Stroobant, Vincent and Brasseur, Robert and Charloteaux, Benoit},
abstractNote = {In this study, we determined the minimal N-terminal fusion peptide of the gp30 of the bovine leukemia virus on the basis of the tilted peptide theory. We first used molecular modelling to predict that the gp30 minimal fusion peptide corresponds to the 15 first residues. Liposome lipid-mixing and leakage assays confirmed that the 15-residue long peptide induces fusion in vitro and that it is the shortest peptide inducing optimal fusion since longer peptides destabilize liposomes to the same extent but not shorter ones. The 15-residue long peptide can thus be considered as the minimal fusion peptide. The effect of mutations reported in the literature was also investigated. Interestingly, mutations related to glycoproteins unable to induce syncytia in cell-cell fusion assays correspond to peptides predicted as non-tilted. The relationship between obliquity and fusogenicity was also confirmed in vitro for one tilted and one non-tilted mutant peptide.},
doi = {10.1016/j.bbrc.2007.01.182},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 355,
place = {United States},
year = {Fri Apr 13 00:00:00 EDT 2007},
month = {Fri Apr 13 00:00:00 EDT 2007}
}