|PROSITE documentation PDOC51538 [for PROSITE entry PS51538]|
Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries [E1]:
- Equine arteritis virus (EAV). - Porcine reproductive and respiratory syndrome virus (PRRSV). - Mice actate dehydrogenase-elevating virus. - Simian hemorrhagic fever virus.
The arterivirus cysteine protease (AV CP) is the most carboxyl-terminally located member of the array of three cysteine proteinase domains present in the amino-terminal 500 residues of the replicase polyproteins. The AV CP is located in the amino-terminal region of nsp2 and is highly conserved among arteriviruses. The cleavage of the nsp2|3 junction appears to be the single processing step mediated by the AV CP. For EAV, it has been shown that cleaved nsp2 is an essential co-factor for cleavage of the nsp4|6 site by the nsp4 proteinase domain (see <PDOC51493>). The AV CP is an unusual Cys protease with amino acid sequence similarities to both papain-like and chymotrypsin-like proteases. The catalytic dyad is composed of Cys and His residues [1,2,3]. The AV CP domain forms peptidase family C33 [E2].
Comparative sequence analysis and site-directed mutagenesis have characterized the AV CP as a cysteine endopeptidase whose conserved domain encompasses about 100 residues. The entire AV CP domain is highly conserved among arteriviruses. Among the conserved residues are a number of cysteines and one aspartate residues .
The profile we developed covers the entire AV CP domain.Last update:
June 2011 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Snijder E.J. Wassenaar A.L.M. Spaan W.J.M. Gorbalenya A.E.|
|Title||The arterivirus Nsp2 protease. An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases.|
|Source||J. Biol. Chem. 270:16671-16676(1995).|
|2||Authors||Wassenaar A.L.M. Spaan W.J.M. Gorbalenya A.E. Snijder E.J.|
|Title||Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease.|
|Source||J. Virol. 71:9313-9322(1997).|
|3||Authors||Ziebuhr J. Snijder E.J. Gorbalenya A.E.|
|Title||Virus-encoded proteinases and proteolytic processing in the Nidovirales.|
|Source||J. Gen. Virol. 81:853-879(2000).|