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Journal of Virology, February 2004, p. 2131-2136, Vol. 78, No. 4
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.4.2131-2136.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Distribution of Hydrophobic Residues Is Crucial for the Fusogenic Properties of the Ebola Virus GP2 Fusion Peptide

B. Adam,1 L. Lins,1 V. Stroobant,2 A. Thomas,1 and R. Brasseur1*

Centre de Biophysique Moléculaire Numérique, FSAGX, 5030 Gembloux,1 Ludwig Institute, UCL, Leuven, Belgium2

Received 9 July 2003/ Accepted 4 November 2003

The lipid-destabilizing properties of the N-terminal domain of the GP2 of Ebola virus were investigated. Our results suggest that the domain of Ebola virus needed for fusion is shorter than that previously reported. The fusogenic properties of this domain are related to its oblique orientation at the lipid/water interface owing to an asymmetric distribution of the hydrophobic residues when helical.

* Corresponding author. Mailing address: Centre de Biophysique Moléculaire Numérique, FSAGX, Passage des Déportés, 2, B-5030 Gembloux, Belgium. Phone: 32-81-622521. Fax: 32-81-622522. E-mail: brasseur.r{at}fsagx.ac.be.

Journal of Virology, February 2004, p. 2131-2136, Vol. 78, No. 4
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.4.2131-2136.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.





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