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Journal of Virology, June 2003, p. 7150-7155, Vol. 77, No. 12
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.12.7150-7155.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

trans Activity of the Norovirus Camberwell Proteinase and Cleavage of the N-Terminal Protein Encoded by ORF1

Ee Ling Seah,1* John A. Marshall,2 and Peter J. Wright1

Department of Microbiology, Monash University, Clayton, Victoria 3800,1 Victorian Infectious Diseases Reference Laboratory, North Melbourne, Victoria 3051, Australia2

Received 3 December 2002/ Accepted 19 March 2003

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 E194/S.

* Corresponding author. Mailing address: Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia. Phone: 61 3 9905 4839. Fax: 61 3 9905 4811. E-mail: Elaine.Seah{at}med.monash.edu.au.

Journal of Virology, June 2003, p. 7150-7155, Vol. 77, No. 12
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.12.7150-7155.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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