NDLI: 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

Content Provider	Springer Nature Link
Author	Xu, Ao Tian Zhou, Yan Jun Li, Guo Xin Yu, Hai Yan, Li Ping Tong, Guang Zhi
Copyright Year	2010
Abstract	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 Cu2+, Zn2+, PMSF and EDTA were significantly inhibitory. His39, Asp64 and Ser118 residues were identified to form the catalytic triad of PRRSV 3CLpro by a series of site-directed mutagenesis analysis.
Starting Page	1905
Ending Page	1910
Page Count	6
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	32
Issue Number	12
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-09-24
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	3C-like proteinase Nsp4 Porcine reproductive and respiratory syndrome virus Biochemistry Applied Microbiology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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