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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

The “Tilted Peptide Theory” Links Membrane Insertion Properties and Fusogenicity of Viral Fusion Peptides

Author(s): B. Charloteaux, A. Lorin, R. Brasseur and L. Lins

Volume 16, Issue 7, 2009

Page: [718 - 725] Pages: 8

DOI: 10.2174/092986609788681724

Price: $65

Abstract

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.

Keywords: Viral fusion, molecular modelling, tilted peptide


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