Charloteaux B, Lorin A, Brasseur R, Lins L
Centre de Biophysique Moléculaire Numérique, Gembloux Agricultural University, 2, passage des déportés, 5030 Gembloux, Belgique.
Protein Pept Lett. 2009;16(7):718-25. doi: 10.2174/092986609788681724.
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.
病毒的I类融合糖蛋白参与病毒包膜与细胞膜之间的融合。这些糖蛋白N端结构域中的一个区域，称为融合肽，对融合至关重要。融合肽能够在体外自行诱导膜融合。在本文中，我们综述了这些肽与融合活性相关的特性，特别是它们倾斜插入膜的能力与融合活性之间存在的相关性。这种关系尤其有助于成功预测一些融合肽足以诱导显著体外融合的最小区域。从现有的病毒融合机制角度讨论了倾斜度和融合活性的概念。
