Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells

@article{Sosnovtsev2006CleavageMA,
  title={Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells},
  author={S. Sosnovtsev and G. Belliot and Kyeong-Ok Chang and Victor G Prikhodko and L. Thackray and C. Wobus and Stephanie M. Karst and H. Virgin and K. Green},
  journal={Journal of Virology},
  year={2006},
  volume={80},
  pages={7816 - 7831}
}
ABSTRACT Murine norovirus (MNV) is presently the only member of the genus Norovirus in the Caliciviridae that can be propagated in cell culture. The goal of this study was to elucidate the proteolytic processing strategy of MNV during an authentic replication cycle in cells. A proteolytic cleavage map of the ORF1 polyprotein was generated, and the virus-encoded 3C-like (3CL) proteinase (Pro) mediated cleavage at five dipeptide cleavage sites, 341E/G342, Q705/N706, 870E/G871, 994E/A995, and… Expand
Differential cleavage of the norovirus polyprotein precursor by two active forms of the viral protease.
Expression of the Murine Norovirus (MNV) ORF1 Polyprotein Is Sufficient to Induce Apoptosis in a Virus-Free Cell Model
Insights into the enzyme-substrate interaction in the norovirus 3C-like protease.
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