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Cloning, characterization and molecular analysis of a metalloprotease from Proteus mirabilis

文献类型：期刊论文

作者Zhang, Weiwei; Han, Qingxi; Liu, Dongyan; Chen, Lingxin
刊名ANNALS OF MICROBIOLOGY
出版日期2011-12-01
卷号61期号:4页码:757-764
关键词Proteus Mirabilis Zapa Enzyme Activity Swarming Motility Proteolysis
ISSN号1590-4261
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
文献子类Article
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.
学科主题Biotechnology & Applied Microbiology ; Microbiology
URL标识查看原文
WOS关键词SWARM-CELL-DIFFERENTIATION ; VIRULENCE FACTOR ; NEISSERIA-MENINGITIDIS ; URINARY-TRACT ; ZAPA ; EXPRESSION ; STRAIN ; PROTEINASES ; SUBSTRATE ; MOTILITY
WOS研究方向Biotechnology & Applied Microbiology ; Microbiology
语种英语
WOS记录号WOS:000296964900007
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
公开日期2012-03-06
源URL[http://ir.yic.ac.cn/handle/133337/5331]  
专题烟台海岸带研究所_山东省海岸带环境工程技术研究中心
烟台海岸带研究所_近岸生态与环境实验室
烟台海岸带研究所_中科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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来源：烟台海岸带研究所

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