Article (Scientific journals)
The "Tilted Peptide Theory" links membrane insertion properties and fusogenicity of viral fusion peptides.
Charloteaux, Benoît; Lorin, Aurélien; Brasseur, Robert et al.
2009In Protein and Peptide Letters, 16 (7), p. 718-25
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Keywords :
Amino Acid Sequence; Humans; Lipid Metabolism; Models, Biological; Molecular Sequence Data; Mutation; Peptides/chemistry/genetics/metabolism; Viral Fusion Proteins/chemistry/genetics/metabolism; Virus Internalization
Abstract :
[en] Class I fusion glycoproteins of viruses are involved in the fusion between viral envelope and cell membrane. A region located in the N-terminal domain of these glycoproteins, called the fusion peptide, is essential for fusion. Fusion peptides are able to induce by themselves in vitro membrane fusion. In this paper, we review the properties of those peptides related to their fusogenicity, in particular the correlation existing between their ability to insert obliquely in membranes and fusogenicity. This relation notably allows predicting successfully the minimal region of some fusion peptides sufficient to induce significant in vitro fusion. The notion of obliquity and fusogenicity is discussed in terms of the existing proposed mechanisms for viral fusion.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Charloteaux, Benoît ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Lorin, Aurélien
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Lins, Laurence  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Language :
English
Title :
The "Tilted Peptide Theory" links membrane insertion properties and fusogenicity of viral fusion peptides.
Publication date :
2009
Journal title :
Protein and Peptide Letters
ISSN :
0929-8665
Publisher :
Bentham Science Publishers Ltd., Hilversum, Netherlands
Volume :
16
Issue :
7
Pages :
718-25
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 23 June 2010

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