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© Charles Dauguet
Virus VIH-2, second virus du sida isolé en 1985 par l'équipe du Pr. Montagnier de l'Institut Pasteur.
Publication : FEBS letters

Pre-transmembrane sequence of Ebola glycoprotein. Interfacial hydrophobicity distribution and interaction with membranes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 01 Jan 2003

Sáez-Cirión A, Gómara MJ, Agirre A, Nieva JL

Link to Pubmed [PMID] – 12505157

FEBS Lett. 2003 Jan;533(1-3):47-53

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 alpha-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 alpha-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.

http://www.ncbi.nlm.nih.gov/pubmed/12505157