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
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 andreplication. We have examined the biochemical prop-erties of PRRSV 3CLpro and identified those aminoacid residues involved in its catalytic activity as aprelude to developing anti-PRRSV strategies. The 3C-like proteinase (3CLpro) of porcine repro-ductive and respiratory syndrome virus (PRRSV) wasexpressed in Escherichia coli and characterized. The optimal temperature and pH for its proteolytic activitywere 8℃ and 7.5, respectively. Na+(1000 mM) andK+(500 mM) were not inhibitory to its activity butCu2+, Zn2+, PMSF and EDTA were significantly inhibitory. His39, Asp64 and Ser118 residues wereidentified to form the catalytic triad of PRRSV 3CLproby a series of site-directed mutagenesis analysis.
氨基酸 3C蛋白酶 猪繁殖与呼吸综合征病毒
Ao-Tian Xu Yan-Jun Zhou Guo-Xin Li Hai Yu Li-Ping Yan Guang-Zhi Tong
Division of Swine Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, No. 518, Ziyue Road,Minhang District, Shanghai 200241, China
国内会议
上海
英文
1-6
2011-10-01（万方平台首次上网日期，不代表论文的发表时间）