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J Gen Virol 78 (1997), 71-75
© 1997 Society for General Microbiology
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Journal of General Virology, Vol 78, 71-75, Copyright © 1997 by Society for General Microbiology

ARTICLES

Expression and characterization of a recombinant murine coronavirus 3C- like proteinase

A Seybert, J Ziebuhr and SG Siddell
Institute of Virology, University of Wurzburg, Germany.

The replication of coronaviruses involves proteolytic processing of the gene 1 translation products, pp1a and pp1ab. One of the key enzymes in this process is predicted to be a virus-encoded 3C-like proteinase. In this report, we describe a bacterial system that has allowed us to express and characterize a recombinant murine coronavirus (MHV-JHM) 3C- like proteinase. The partially purified protein has been shown to exhibit proteolytic activity in trans and mutation analysis has been used to demonstrate the indispensability of Cys-3495 for enzymatic activity. Finally, the effect of class-specific proteinase inhibitors on the trans cleavage activity of the MHV 3C-like proteinase has been used to demonstrate the functional and structural homology of this enzyme to the picornavirus 3C proteinases.


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