Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1.

@article{Probst1997Proteinase3P,
  title={Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1.},
  author={Christian Probst and M. Jecht and Verena Gauss-M{\"u}ller},
  journal={Journal of virology},
  year={1997},
  volume={71 4},
  pages={3288-92}
}
Two prominent features distinguish hepatitis A virus (HAV) from other members of the picornavirus family. A C-terminally prolonged precursor of the structural protein VP1 is incorporated into assembly intermediates (e.g., the provirion), and a single proteinase is contained within the HAV polyprotein. Using an in vivo expression system, we show that proteolytic liberation of VP1 from its precursors P1-2A and VP1-2A is catalyzed by the virus-encoded proteinase 3Cpro. Among the proposed cleavage… CONTINUE READING