Abstract
Duck hepatitis B virus particles bearing the L and S envelope proteins bind a cellular glycoprotein of 180 kDa (gp180) with high affinity and specificity. Binding is mediated by the pre-S region of the L protein and is blocked by neutralizing but not by non-neutralizing monoclonal antibodies to the virus. These and other properties have suggested that gp180 may be a component of the viral entry machinery. Here we report the purification of gp180 from duck liver and the isolation and characterization of cDNA encoding it. DNA sequence analysis of this cDNA indicates that gp180 is a novel member of the basic carboxypeptidase gene family.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carboxypeptidases / biosynthesis
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Carboxypeptidases / genetics*
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Carboxypeptidases / metabolism*
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Cell Line
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Cloning, Molecular
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Ducks
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Gene Products, env / metabolism
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Hepatitis B Virus, Duck / physiology*
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Humans
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Liver / metabolism*
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Liver / virology*
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Membrane Glycoproteins / biosynthesis
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Membrane Glycoproteins / genetics*
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Membrane Glycoproteins / metabolism*
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Molecular Sequence Data
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Multigene Family*
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Oligodeoxyribonucleotides
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Proteins*
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Restriction Mapping
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Sequence Homology, Amino Acid
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Transfection
Substances
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Gene Products, env
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Membrane Glycoproteins
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Oligodeoxyribonucleotides
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Peptide Fragments
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Proteins
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Carboxypeptidases
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metallocarboxypeptidase D