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Trans activity of the norovirus Camberwell proteinase and cleavage of the N-terminal protein encoded by ORF1.

ABSTRACT: The virus-encoded proteinase of Camberwell virus, a genogroup 2 norovirus, was synthesized in Escherichia coli. The purified proteinase had correct N and C termini and showed trans activity in cell-free assays. trans activity was also demonstrated in COS cells transfected with constructs encoding either the proteinase or a proteinase-polymerase fusion. The N-terminal protein of ORF1 was cleaved in COS cells, possibly at the site E(194)/S.

SUBMITTER: Seah EL

PROVIDER: S-EPMC156193 | biostudies-literature | 2003 Jun

REPOSITORIES: biostudies-literature

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Trans activity of the norovirus Camberwell proteinase and cleavage of the N-terminal protein encoded by ORF1.

Seah Ee Ling EL Marshall John A JA Wright Peter J PJ

Journal of virology 20030601 12

The virus-encoded proteinase of Camberwell virus, a genogroup 2 norovirus, was synthesized in Escherichia coli. The purified proteinase had correct N and C termini and showed trans activity in cell-free assays. trans activity was also demonstrated in COS cells transfected with constructs encoding either the proteinase or a proteinase-polymerase fusion. The N-terminal protein of ORF1 was cleaved in COS cells, possibly at the site E(194)/S. ...[more]

PMID: 12768037

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