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Journal of Virology, April 2005, p. 5142-5152, Vol. 79, No. 8
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.8.5142-5152.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Instituto de Biología Molecular y Celular, Universidad "Miguel Hernández," Elche-Alicante, Spain
Received 24 August 2004/ Accepted 5 November 2004
The human immunodeficiency virus gp41 envelope protein mediates the entry of the virus into the target cell by promoting membrane fusion. In order to gain new insights into the viral fusion mechanism, we studied a 35-residue peptide pertaining to the loop domain of gp41, both in solution and membrane bound, by using infrared and fluorescence spectroscopy. We show here that the peptide, which has a membrane-interacting surface, binds and interacts with phospholipid model membranes and tends to aggregate in the presence of a membranous medium and induce the leakage of vesicle contents. The results reported in this work, i.e., the destabilization and fusion of negatively charged model membranes, suggest an essential role of the loop domain in the membrane fusion process induced by gp41.
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