title: 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.
authors.affiliation: Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia. Elaine.Seah@med.monash.edu.au
authors.forename: Ee Ling
authors.initials: EL
authors.lastname: Seah
authors.forename: John A
authors.initials: JA
authors.lastname: Marshall
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Wright
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002139:Caliciviridae / Q000201:enzymology* / Q000235:genetics; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D014162:Transfection
chemical_list: D010450:Endopeptidases