Protease digestion of hepatitis A virus: disparate effects on capsid proteins, antigenicity, and infectivity.
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.
Lemon
S M
SM
Department of Medicine, University of North Carolina, Chapel Hill 27599-7030.
Amphlett
E
E
Sangar
D
D
D000818:Animals; D000911:Antibodies, Monoclonal; D000956:Antigens, Viral / Q000032:analysis; D002213:Capsid / Q000378:metabolism*; D036022:Capsid Proteins; D002460:Cell Line; D002918:Chymotrypsin / Q000494:pharmacology; D010450:Endopeptidases / Q000494:pharmacology*; D004797:Enzyme-Linked Immunosorbent Assay; D006507:Hepatovirus / Q000187:drug effects / Q000276:immunology / Q000502:physiology*; D006358:Hot Temperature; D007700:Kinetics; D014357:Trypsin / Q000378:metabolism / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D036022:Capsid Proteins; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin