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- Title
Characterization of the biochemical properties and identification of amino acids forming the catalytic center of 3C-like proteinase of porcine reproductive and respiratory syndrome virus.
- Authors
Ao-Tian Xu; Yan-Jun Zhou; Guo-Xin Li; Hai Yu; Li-Ping Yan; Guang-Zhi Tong
- Abstract
Purpose of work: The non-structural protein 4 (Nsp4) of porcine reproductive and respiratory syndrome virus (PRRSV) functions as a 3C-like proteinase (3CLpro) and plays a pivotal role in gene expression and replication. We have examined the biochemical properties of PRRSV 3CLpro and identified those amino acid residues involved in its catalytic activity as a prelude to developing anti-PRRSV strategies. The 3C-like proteinase (3CLpro) of porcine reproductive and respiratory syndrome virus (PRRSV) was expressed in Escherichia coli and characterized. The optimal temperature and pH for its proteolytic activity were 8°C and 7.5, respectively. Na (1000 mM) and K (500 mM) were not inhibitory to its activity but Cu, Zn, PMSF and EDTA were significantly inhibitory. His, Asp and Ser residues were identified to form the catalytic triad of PRRSV 3CLpro by a series of site-directed mutagenesis analysis.
- Subjects
AMINO acids; PROTEINASES; PORCINE reproductive &; respiratory syndrome; PROTEINS; BIOCHEMISTRY
- Publication
Biotechnology Letters, 2010, Vol 32, Issue 12, p1905
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-010-0370-1