ORBi: Charloteaux Benoît - The N-terminal 12 residue long peptide of HIV gp41 is the minimal peptide sufficient to induce significant T-cell-like membrane destabilization in vitro.

Reference : The N-terminal 12 residue long peptide of HIV gp41 is the minimal peptide sufficient to ...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/63378

Title :	The N-terminal 12 residue long peptide of HIV gp41 is the minimal peptide sufficient to induce significant T-cell-like membrane destabilization in vitro.
Language :	English
Author, co-author :	Charloteaux, Benoît [Université de Liège > > Gembloux Agro-Bio Tech >]
	Lorin, A. [> > > >]
	Crowet, Jean-Marc [Université de Liège > > Gembloux Agro-Bio Tech >]
	Stroobant, V. [> > > >]
	Lins, Laurence [Université de Liège > > Gembloux Agro-Bio Tech >]
	Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
	Brasseur, Robert [Université de Liège > > Gembloux Agro-Bio Tech >]
Publication date :	2006
Journal title :	Journal of molecular biology
Volume :	359
Issue/season :	3
Pages :	597-609
Audience :	International
ISSN :	0022-2836
Abstract :	[en] Here, we predicted the minimal N-terminal fragment of gp41 required to induce significant membrane destabilization using IMPALA. This algorithm is dedicated to predict peptide interaction with a membrane. We based our prediction of the minimal fusion peptide on the tilted peptide theory. This theory proposes that some protein fragments having a peculiar distribution of hydrophobicity adopt a tilted orientation at a hydrophobic/hydrophilic interface. As a result of this orientation, tilted peptides should disrupt the interface. We analysed in silico the membrane-interacting properties of gp41 N-terminal peptides of different length derived from the isolate BRU and from an alignment of 710 HIV strains available on the Los Alamos National Laboratory. Molecular modelling results indicated that the 12 residue long peptide should be the minimal fusion peptide. We then assayed lipid-mixing and leakage of T-cell-like liposomes with N-terminal peptides of different length as first challenge of our predictions. Experimental results confirmed that the 12 residue long peptide is necessary and sufficient to induce membrane destabilization to the same extent as the 23 residue long fusion peptide. In silico analysis of some fusion-incompetent mutants presented in the literature further revealed that they cannot insert into a modelled membrane correctly tilted. According to this work, the tilted peptide model appears to explain at least partly the membrane destabilization properties of HIV fusion peptide.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/63378
DOI :	10.1016/j.jmb.2006.04.018

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