FEBS Letters | |
Pre‐transmembrane sequence of Ebola glycoprotein | |
Agirre, Aitziber1  Sáez-Cirión, Asier1  Nieva, José L1  Gómara, Marı́a J1  | |
[1] Unidad de Biofı́sica (CSIC-UPV/EHU) and Departamento de Bioquı́mica, Universidad del Paı́s Vasco, Aptdo. 644, 48080 Bilbao, Spain | |
关键词: Viral fusion protein; Interfacial hydrophobicity; Protein–lipid interaction; Infrared spectroscopy; Ebola GP2; ANTS; 8-aminonaphthalene-1; 3; 6-trisulfonic acid; CHOL; cholesterol; DPX; p-xylenebis(pyridinium)bromide; IR; infrared spectroscopy; EBOc; synthetic sequence (20 aa) representing residues 640–657 of Ebola GP precursor (Zaire strain; GenBank accession no. U31033); EBOscr; scrambled EBOc; LUV; large unilamellar vesicles; PC; phosphatidylcholine; PE; phosphatidylethanolamine; SM; sphingomyelin; | |
DOI : 10.1016/S0014-5793(02)03747-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The membrane-interacting domain that precedes the transmembrane anchor of Ebola glycoprotein has been characterized. This aromatic-rich region is predicted to bind the membrane interface adopting an α-helical structure. Peptides representing either the Ebola glycoprotein pre-transmembrane sequence, or a ‘scrambled’ control with a different hydrophobic-at-interface moment, have been studied. Insertion into lipid monolayers, changes in intrinsic fluorescence and in infrared spectra demonstrated that only the wild-type peptide bound the interface under equilibrium conditions and adopted an α-helical conformation. The presence of the raft-associated lipid sphingomyelin did not affect membrane insertion, but it stimulated highly the membrane-destabilizing capacity of the pre-transmembrane sequence. A parallel study of the effects of the viral sequence and of melittin suggests that Ebola glycoprotein pre-transmembrane sequence might target membranes inherently prone to destabilization by lytic peptides.
【 授权许可】
Unknown
【 预 览 】
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