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J. Biol. Chem., Vol. 276, Issue 39, 36613-36623, September 28, 2001
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From the TECNOGEN S.C.p.A., Parco Scientifico, 81015 Piana di Monte
Verna (CE), Caserta 81015, Italy and A direct involvement of the hepatitis B virus
(HBV) preS1-(21-47) sequence in virus attachment to cell
membrane receptor(s) and the presence on the plasma membranes of HepG2
cells of protein(s) with receptor activity for HBV have been suggested
by many previous experiments. In this study, by using a tetravalent
derivative of the preS1-(21-47) sequence, we have isolated by affinity
chromatography from detergent-solubilized HepG2 plasma membranes a
44-kDa protein (HBV-binding protein; HBV-BP), which was found to
closely correspond to the human squamous cell carcinoma antigen 1 (SCCA1), a member of the ovalbumin family of serine protease
inhibitors. Comparison of SCCA1 sequence with the sequence of the
corresponding HBV-BP cDNA, cloned by polymerase chain reaction
starting from RNA poly(A)+ fractions extracted from
HepG2 cells, indicated the presence of only four nucleotide
substitutions in the coding region, leading to three amino acid
changes. Intact recombinant HBV-BP lacked inhibitory activity for
serine proteases such as
Cloning and Expression of a Novel Hepatitis B
Virus-binding Protein from HepG2 Cells*
,,, and Università
degli Studi di Padova, Dipartimento di Medicina Clinica e Sperimentale,
Clinica Medica 5, 35128 Padova, Italy
-chymotrypsin and trypsin but inhibited
with high potency cysteine proteases such as papain and cathepsin L. Direct binding experiments confirmed the interaction of recombinant
HBV-BP with the HBV preS1 domain. HepG2 cells overexpressing HBV-BP
after transfection of corresponding cDNA showed a virus binding
capacity increased by 2 orders of magnitude compared with untransfected
cells, while Chinese hamster ovary cells, which normally do not bind to
HBV, acquired susceptibility to HBV binding after transfection. Native
HBV particle entry was enhanced in transfected cells. Both recombinant
HBV-BP and antibodies to recombinant HBV-BP blocked virus binding and
internalization in transfected cells as well as in primary human
hepatocytes in a dose-dependent manner. Our findings
suggest that this protein plays a major role in HBV infection.
*
This research was performed under a contract of the Italian
Ministero dell'Università della Ricerca Scientifica e
Tecnologica assigned to TECNOGEN s.c.p.a. within the "Programma
Nazionale di Ricerca sui Sistemi Neurobiologici-Tecnologie della
Trasduzione del Segnale."The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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