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
| العنوان: | 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 |
|---|---|
| المؤلفون: | Hai Yu, Guoxin Li, Liping Yan, Yan-Jun Zhou, Ao-Tian Xu, Guangzhi Tong |
| المصدر: | Biotechnology Letters |
| بيانات النشر: | Springer Netherlands, 2010. |
| سنة النشر: | 2010 |
| مصطلحات موضوعية: | animal diseases, viruses, Nsp4, Mutagenesis (molecular biology technique), Gene Expression, Bioengineering, Viral Nonstructural Proteins, medicine.disease_cause, Applied Microbiology and Biotechnology, Virus, chemistry.chemical_compound, Catalytic Domain, Catalytic triad, Enzyme Stability, medicine, Escherichia coli, Porcine respiratory and reproductive syndrome virus, Amino Acids, Enzyme Inhibitors, chemistry.chemical_classification, biology, 3C-like proteinase, General Medicine, Hydrogen-Ion Concentration, Porcine reproductive and respiratory syndrome virus, biology.organism_classification, Recombinant Proteins, Amino acid, Original Research Paper, Cold Temperature, Cysteine Endopeptidases, Enzyme, chemistry, Biochemistry, Mutagenesis, Site-Directed, PMSF, Biotechnology |
| الوصف: | 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 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. Electronic supplementary material The online version of this article (doi:10.1007/s10529-010-0370-1) contains supplementary material, which is available to authorized users. |
| اللغة: | English |
| تدمد: | 1573-6776 0141-5492 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fc270672434724640425b056fd4f04dTest http://europepmc.org/articles/PMC7088359Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....2fc270672434724640425b056fd4f04d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15736776 01415492 |
|---|