| 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. | |
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MedLine Citation:
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PMID: 20865444 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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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(2+), Zn(2+), PMSF and EDTA were significantly inhibitory. His(39), Asp(64) and Ser(118) residues were identified to form the catalytic triad of PRRSV 3CLpro by a series of site-directed mutagenesis analysis. |
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Authors:
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Ao-Tian Xu; Yan-Jun Zhou; Guo-Xin Li; Hai Yu; Li-Ping Yan; Guang-Zhi Tong |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-09-24 |
Journal Detail:
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Title: Biotechnology letters Volume: 32 ISSN: 1573-6776 ISO Abbreviation: Biotechnol. Lett. Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-05 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8008051 Medline TA: Biotechnol Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 1905-10 Citation Subset: IM |
Affiliation:
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Division of Swine Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, No. 518, Ziyue Road, Minhang District, Shanghai, 200241, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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