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1 Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense, 28040 Madrid
2 Centro Nacional de Biotecnología, Unidad de Inmunología, CSIC-Pharmacia, Universidad Autónoma, 28049 Madrid, Spain
and3 Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond, VA 23298, USA
One of the first steps in the infective cycle of an enveloped virus consists of the fusion of the viral and cellular membranes. This process is usually achieved as a result of membrane destabilization brought about by a viral fusion peptide located at the amino terminus of one of the viral envelope glycoproteins. Previous sequence similarity studies by Rodriguez-Crespo et al. (Journal of General Virology 75, 637–639, 1994) have shown that a hydrophobic stretch in the amino-terminal sequence of the S protein of hepatitis B virus shares several characteristics with fusion peptides of retroviruses and paramyxoviruses. A 16 residue peptide with this sequence was synthesized and its interaction with liposomes characterized. This peptide was able to mediate vesicle aggregation, lipid mixing and liposome leakage in a pH dependent manner at concentrations ranging from 3·5 to 52·0 µM. These effects were specific for negatively charged phospholipid vesicles. The peptide was also able to haemolyse erythrocytes. This study supports the notion that the sequence might be important in the initial infective steps of this virus, interacting with the target membranes and bringing about their subsequent destabilization.
* Author for correspondence. Fax +34 1 3944159. e-mail pacog@solea.quim.ucm.es
Received 9 August 1994;
accepted 5 October 1994.
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