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Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion
Tatiana Suárez1, María J Gómara, Félix M Goñi
1Unidad de Biofísica (CSIC-UPV/EHU) y Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080, Bilbao, Spain.
Abstract:
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 alpha-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 beta-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.
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