Protease digestion of hepatitis A virus cleaves capsid protein VP2 without significantly reducing infectivity or antigenicity, indicating a protease-accessible surface site not critical for receptor attachment or dominant antigenicity.
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May inform HAV capsid engineering strategies; leaves open translation beyond animal models.
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.
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Lemon et al. (1991) studied this question.
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