Abstract
High concentrations of either trypsin or chymotrypsin caused nearly complete cleavage of capsid protein VP2 of hepatitis A virus but did not significantly reduce the infectivity, thermostability, or antigenicity of the virus. Chymotrypsin also had a lesser effect on VP1. These findings indicate the presence of a protease-accessible VP2 surface site which neither contributes significantly to the dominant antigenic site nor plays a role in the attachment of the virus to putative cell receptors.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Antibodies, Monoclonal
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Antigens, Viral / analysis
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Capsid / metabolism*
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Capsid Proteins
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Cell Line
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Chymotrypsin / pharmacology
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Endopeptidases / pharmacology*
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Enzyme-Linked Immunosorbent Assay
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Hepatovirus / drug effects
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Hepatovirus / immunology
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Hepatovirus / physiology*
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Hot Temperature
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Kinetics
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Trypsin / metabolism
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Trypsin / pharmacology
Substances
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Antibodies, Monoclonal
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Antigens, Viral
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Capsid Proteins
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Endopeptidases
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Chymotrypsin
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Trypsin