The "Tilted Peptide Theory" links membrane insertion properties and fusogenicity of viral fusion peptides.
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.
Charloteaux
B
B
Centre de Biophysique Moléculaire Numérique, Gembloux Agricultural University, 2, passage des déportés, 5030 Gembloux, Belgique.
Lorin
A
A
Brasseur
R
R
Lins
L
L
D000595:Amino Acid Sequence; D006801:Humans; D050356:Lipid Metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D053586:Virus Internalization
D010455:Peptides; D014760:Viral Fusion Proteins