Calcium‐dependent conformational changes of membrane‐bound Ebola fusion peptide drive vesicle fusion

FEBS Letters

Mingarro, Ismael¹  Goñi, Félix M²  Suárez, Tatiana²  Muga, Arturo²  Pérez-Payá, Enrique¹  Nieva, José L²  Gómara, Marı́a J² 

[1] Departament de Bioquı́mica i Biologia Molecular, Universitat de València, E-46100 Burjassot, València, Spain;Unidad de Biofı́sica (CSIC-UPV/EHU) y Departamento de Bioquı́mica, Universidad del Paı́s Vasco, Aptdo. 644, 48080, Bilbao, Spain

关键词: Ebola glycoprotein;    Fusion peptide;    Membrane fusion;    Viral fusion;    Peptide–lipid interaction;   

DOI  :  10.1016/S0014-5793(02)03847-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The fusogenic subdomain of the Ebola virus envelope glycoprotein is an internal sequence located ca. 20 residues downstream the N-terminus of the glycoprotein transmembrane subunit. Partitioning of the Ebola fusion peptide into membranes containing phosphatidylinositol in the absence of Ca²⁺ stabilizes an α-helical conformation, and gives rise to vesicle efflux but not vesicle fusion. In the presence of millimolar Ca²⁺ the membrane-bound peptide adopts an extended β-structure, and induces inter-vesicle mixing of lipids. The peptide conformational polymorphism may be related to the flexibility of the virus–cell intermembrane fusogenic complex.

【 授权许可】

Unknown