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J. Virol. doi:10.1128/JVI.01270-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

IDENTIFICATION AND CHARACTERIZATION OF PEPTIDES THAT INTERACT WITH HEPATITIS B VIRUS VIA THE PUTATIVE RECEPTOR BINDING SITE

State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Unité de Pathogenese des Hépatites Virales B et Immunothérapie, INSERM U812/Institut Pasteur, 75724 Paris, France; Ruijin Hospital, Department of Infectious Diseases, Shanghai 200025, China; Unité Postulante des Hépacivirus, Institut Pasteur, 75724 Paris, France; Unité d'Organisation Nucléaire et Oncogénèse, INSERM U579/Institut Pasteur, 75724 Paris, France

^* To whom correspondence should be addressed. Email: wangy{at}sibs.ac.cn. yhxie{at}sibs.ac.cn.

	Abstract

A direct involvement of the PreS domain of hepatitis B virus (HBV) large envelope protein, and in particular amino acid residues 21-47 has been suggested by many previous studies in virus attachment to hepatocytes. Several PreS-interacting proteins have been identified. However, they share few common sequence motifs and a bona fide cellular receptor for HBV remains elusive. In this study, we aimed to identify PreS-interacting motifs and to search for novel HBV-interacting proteins and the long-sought receptor. PreS fusion proteins were used as baits to screen a phage display library of random peptides. A group of PreS-binding peptides were obtained. These peptides could bind to aa21-47 of PreS1 and shared a linear motif (-W₁T₂X₃W₄W₅-) sufficient for binding specifically to PreS and viral particles. Several human proteins with such a motif were identified through BLAST search. Analysis of their biochemical and structural properties suggested that lipoprotein lipase (LPL), a key enzyme in lipoprotein metabolism, might interact with PreS and HBV particles. The interaction of HBV with LPL was respectively demonstrated by in vitro binding, virus capture and cell attachment assays. These findings suggest that LPL may play a role in the initiation of HBV infection. Identification of peptides and protein ligands corresponding to LPL that bind to HBV envelope will offer new therapeutic strategies against HBV infection.

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