Hepatitis B virus (HBV) binding factor in human serum: candidate for a soluble form of hepatocyte HBV receptor

Budkowska, Agata; Quan, Canh P.; Groh, F; Bedossa, P.; Dubreuil, Pascal; Jp, Bouvet; Pillot, J.

doi:10.1128/jvi.67.7.4316-4322.1993

Cited by 44 publications

(19 citation statements)

References 31 publications

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“…We have described in human serum a 50-kDa moletive translational initiation sites. The domains of the M cule, called ''HBV-binding factor'' (HBV-BF) which interand L proteins, encoded by the pre-S1 and pre-S2 fragacts with the pre-S1 and pre-S2 epitopes of the viral envelope (5). The immunochemical properties of this mol-teins, and the localization of an antigenically related com-Superose 12 column (Pharmacia) and by SDS-PAGE.…”

Section: Introductionmentioning

confidence: 99%

Activation of the Envelope Proteins by a Metalloproteinase Enables Attachment and Entry of the Hepatitis B Virus into T-Lymphocyte

et al. 1997

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Previously, we identified an HBV binding factor (HBV-BF), a 50-kDa serum glycoprotein which interacts with HBV envelope proteins and which is also located in the membrane of normal human hepatocyte (A. Budkowska et al. (1993) J. Virol. 67, 4316). Here we show that HBV-BF is a neutral metalloproteinase which shares substrate specificity and properties with a newly described family of membrane type matrix metalloproteinases. HBV-BF treatment of the HBV resulted in the cleavage of the N-terminal part of the middle HBV envelope protein at the pre-S2(136-141) amino acid sequence VRGLYF/L (containing a single arginine cleavage site). HBV-BF affected the reactivity of the large HBV protein with pre-S1-specific MAbs, probably inducing the conformational change of the pre-S1 domain. The HBV-BF-digested virus remained morphologically intact with unchanged S antigenic determinants. The structural modifications of the viral envelope proteins induced by HBV-BF enabled cell membrane attachment and viral entry into the T-lymphocyte. Both processes were blocked by the metalloproteinase inhibitor 1,10 phenanthroline. Thus, the host-dependent proteolytic activation of the envelope proteins seems to be essential for the HBV entry into the cell. HBV-BF under a membrane bound or a secreted form could be (one of) the molecule(s) responsible for the HBV proteolytic activation.

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Section: Introductionmentioning

confidence: 99%

Activation of the Envelope Proteins by a Metalloproteinase Enables Attachment and Entry of the Hepatitis B Virus into T-Lymphocyte

et al. 1997

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“…Since the pre-S domain represents the sequence unique to the large envelope protein, it is believed to contain the hepatocyte receptor-binding site. Several cellular proteins which bind to the envelope proteins of HBV through the pre-S or S domain have recently been reported (1,2,10,20,21,23), but it has been difficult to firmly establish that such proteins are components of the viral receptor.…”

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confidence: 99%

Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection

Tong

Wands

1995

J Virol

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Identification of cell surface viral binding proteins is important for understanding viral attachment and internalization. We have fused the pre-S domain of the duck hepatitis B virus (DHBV) large envelope protein to glutathione S-transferase and demonstrated a 170-kDa binding protein (p170) in [ 35 S]methionine-labeled duck hepatocyte lysates. This glycoprotein was found abundantly in all extrahepatic tissues infectible withDHBV and in some noninfectible tissues, though it is not secreted into the blood. The interaction of pre-S fusion protein with p170 was competitively inhibited by wild-type DHBV in a dose-dependent manner. In addition, infection of hepatocytes with DHBV blocked the binding of pre-S fusion protein to p170, which suggests a biological role for p170 during natural infection. The p170 binding site was mapped to a conserved sequence of 16 amino acid residues (positions 87 to 102) by using 24 pre-S deletion mutants; this binding domain coincides with a major virus-neutralizing antibody epitope. Furthermore, site-directed mutagenesis revealed that an arginine residue at position 97 is critical for p170 binding. p170 was purified by a combination of ion-exchange and affinity chromatographies, and four peptide sequences were obtained. Two peptides showed significant similarities to human and animal carboxypeptidases H, M, and N. Taken together, these results raise the possibility that the p170 binding protein is important during the replication cycle of DHBV.

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“…HBsAg is the main factor during the interaction of HBV with hepatocytes, and HBsAg has been demonstrated to be important for the formation of infectious virus particles and for receptor interaction [24,27,47]. The hepatocyte binding domain has been mapped to preS region [24,[48][49][50][51][52][53][54]. We have taken advantage of the target characteristic of preS protein for hepatocytes and the function of the liposome to protect plasmid DNA against the DNase digestion.…”

Section: Discussionmentioning

confidence: 99%

Gene delivery into hepatocytes with the preS/liposome/DNA system

Wang

Yuan

Jin

2008

Biotechnology Journal

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Gene delivery into human hepatocytes remains a critical issue for the development of liver-directed gene therapy. Gene delivery based on non-viral vectors is an attractive approach relative to viral vectors. In this report, novel delivery system of preS/liposome/DNA virus-like particle (VLP) was developed for gene transfection into hepatocytes in vivo and in vitro. Plasmid pCMVβ, expressing β-galactosidase, was encapsulated with cationic liposome, and then the histidine-tagged preS domain of hepatitis B virus was coated on the surface of liposome/DNA to form preS/liposome/DNA VLP. Transfection efficiencies of preS/liposome/DNA, liposome/DNA, naked DNA and preS were analyzed using several different human cell lines. The highest transfection efficiency was found using preS/liposome/DNA VLP as the transfection reagent in human hepatocyte (HH) cell line. Results show that preS domain of hepatitis B virus coated on liposome/DNA can be used for highly efficient gene transfection into human hepatocytes. Moreover, the target characteristic of preS/liposome/DNA was analyzed in vivo. After preS/liposome/DNA VLP was injected into immunocompromised (Nude) mice via the tail vein, most of β-galactosidase was expressed in the liver; however, no significant target expression was found with the injection of liposome/DNA or naked DNA. Our results show that preS/liposome/DNA VLP can be used as a novel liver-specific gene delivery system.

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Hepatitis B virus (HBV) binding factor in human serum: candidate for a soluble form of hepatocyte HBV receptor

Cited by 44 publications

References 31 publications

Activation of the Envelope Proteins by a Metalloproteinase Enables Attachment and Entry of the Hepatitis B Virus into T-Lymphocyte

Activation of the Envelope Proteins by a Metalloproteinase Enables Attachment and Entry of the Hepatitis B Virus into T-Lymphocyte

Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection

Gene delivery into hepatocytes with the preS/liposome/DNA system

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