| Cloning, characterization and molecular analysis of a metalloprotease from Proteus mirabilis | |
Zhang, Weiwei; Han, Qingxi ; Liu, Dongyan; Chen, Lingxin
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| 发表期刊 | ANNALS OF MICROBIOLOGY
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| ISSN | 1590-4261 |
| 2011-12-01 | |
| 卷号 | 61期号:4页码:757-764 |
| 关键词 | Proteus Mirabilis Zapa Enzyme Activity Swarming Motility Proteolysis |
| 产权排序 | [Zhang, Weiwei; Han, Qingxi; Liu, Dongyan; Chen, Lingxin] Chinese Acad Sci, Key Lab Coastal Environm Proc, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China |
| 通讯作者 | Chen, LX (reprint author), Chinese Acad Sci, Key Lab Coastal Environm Proc, Yantai Inst Coastal Zone Res, 17 Chunhui Rd, Yantai 264003, Peoples R China |
| 作者部门 | 环境化学实验室 |
| 英文摘要 | Proteus mirabilis is an important pathogen that is usually found in complicated urinary tracts infection. It possesses a metalloprotease, ZapA, that acts as a virulence factor. The gene encoding ZapA was cloned from P. mirabilis Pm7-a strain isolated from marine environments-and conditionally expressed in Escherichia coli. Zn(2+) and Co(2+) exhibited an apparently positive effect on the enzyme activity of the 54-kDa protease. Ag(+), Cd(2+), Cu(2+), Hg(2+), Pb(2+), EDTA and sulfhydryl reagents including beta-mercaptoethanol and dithiothreitol exhibited an apparently negative effect on enzyme activity. Enzyme activity analysis revealed that the optimum temperature and pH for purified recombinant ZapA were approximately 40 degrees C and 8.0, respectively. Enzyme activity and western immuno-blotting analysis were used for the determination of the extracellular location of ZapA. The simultaneously depressed expression of zapA and swarming motility of Pm7 in the presence of glucose were determined by real-time PCR and swarming motility measurements, respectively. Furthermore, the outer membrane proteins of two bacteria (Enterobacter sp. T41 and Edwardsiella tarda strain TX1-a fish pathogen) were found to be substrates of ZapA proteolysis.; Proteus mirabilis is an important pathogen that is usually found in complicated urinary tracts infection. It possesses a metalloprotease, ZapA, that acts as a virulence factor. The gene encoding ZapA was cloned from P. mirabilis Pm7-a strain isolated from marine environments-and conditionally expressed in Escherichia coli. Zn(2+) and Co(2+) exhibited an apparently positive effect on the enzyme activity of the 54-kDa protease. Ag(+), Cd(2+), Cu(2+), Hg(2+), Pb(2+), EDTA and sulfhydryl reagents including beta-mercaptoethanol and dithiothreitol exhibited an apparently negative effect on enzyme activity. Enzyme activity analysis revealed that the optimum temperature and pH for purified recombinant ZapA were approximately 40 degrees C and 8.0, respectively. Enzyme activity and western immuno-blotting analysis were used for the determination of the extracellular location of ZapA. The simultaneously depressed expression of zapA and swarming motility of Pm7 in the presence of glucose were determined by real-time PCR and swarming motility measurements, respectively. Furthermore, the outer membrane proteins of two bacteria (Enterobacter sp. T41 and Edwardsiella tarda strain TX1-a fish pathogen) were found to be substrates of ZapA proteolysis. |
| 文章类型 | Article |
| 资助机构 | National Natural Science Foundation of China (NSFC)[20975089]; Department of Science and Technology of Shandong Province[2008GG20005005]; Department of Science and Technology of Yantai City of China[2010235]; Chinese Academy of Sciences[KZCX2-EW-206, KZCX2-YW-Q07-04, Kf201012]; Key Laboratory of Experimental Marine Biology; Institute of Oceanology |
| 收录类别 | SCI |
| 语种 | 英语 |
| 关键词[WOS] | SWARM-CELL-DIFFERENTIATION ; VIRULENCE FACTOR ; NEISSERIA-MENINGITIDIS ; URINARY-TRACT ; ZAPA ; EXPRESSION ; STRAIN ; PROTEINASES ; SUBSTRATE ; MOTILITY |
| 研究领域[WOS] | Biotechnology & Applied Microbiology ; Microbiology |
| WOS记录号 | WOS:000296964900007 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.yic.ac.cn/handle/133337/5330 |
| 专题 | 中国科学院海岸带环境过程与生态修复重点实验室_海岸带环境工程技术研究与发展中心 中国科学院海岸带环境过程与生态修复重点实验室_海岸带环境过程实验室 中国科学院海岸带环境过程与生态修复重点实验室 |
| 作者单位 | Chinese Acad Sci, Key Lab Coastal Environm Proc, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Weiwei,Han, Qingxi,Liu, Dongyan,et al. Cloning, characterization and molecular analysis of a metalloprotease from Proteus mirabilis[J]. ANNALS OF MICROBIOLOGY,2011,61(4):757-764. |
| APA | Zhang, Weiwei,Han, Qingxi,Liu, Dongyan,&Chen, Lingxin.(2011).Cloning, characterization and molecular analysis of a metalloprotease from Proteus mirabilis.ANNALS OF MICROBIOLOGY,61(4),757-764. |
| MLA | Zhang, Weiwei,et al."Cloning, characterization and molecular analysis of a metalloprotease from Proteus mirabilis".ANNALS OF MICROBIOLOGY 61.4(2011):757-764. |
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