Pre‐transmembrane sequence of Ebola glycoprotein

FEBS Letters

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