Conservation of substrate specificities among coronavirus main proteases
Top Cited Papers
- 1 March 2002
- journal article
- Published by Microbiology Society in Journal of General Virology
- Vol. 83 (3) , 595-599
- https://doi.org/10.1099/0022-1317-83-3-595
Abstract
The key enzyme in coronavirus replicase polyprotein processing is the coronavirus main protease, 3CLpro. The substrate specificities of five coronavirus main proteases, including the prototypic enzymes from the coronavirus groups I, II and III, were characterized. Recombinant main proteases of human coronavirus (HCoV), transmissible gastroenteritis virus (TGEV), feline infectious peritonitis virus, avian infectious bronchitis virus and mouse hepatitis virus (MHV) were tested in peptide-basedtrans-cleavage assays. The determination of relative rate constants for a set of corresponding HCoV, TGEV and MHV 3CLprocleavage sites revealed a conserved ranking of these sites. Furthermore, a synthetic peptide representing the N-terminal HCoV 3CLprocleavage site was shown to be effectively hydrolysed by noncognate main proteases. The data show that the differential cleavage kinetics of sites within pp1a/pp1ab are a conserved feature of coronavirus main proteases and lead us to predict similar processing kinetics for the replicase polyproteins of all coronaviruses.Keywords
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