Biochemical Characterization of the Outer Membrane Enzyme OMPLA from Riemerella anatipestifer

被引：0

作者：

Liao, Shenquan ^{[1
]}

Yuan, Jianfeng ^{[1
]}

Qin, Zonghua ^{[1
]}

Wu, Caiyan ^{[1
]}

Lv, Minna ^{[1
]}

Qi, Nanshan ^{[1
]}

Cai, Jianping ^{[1
]}

Sun, Mingfei ^{[1
]}

机构：

[1] Guangdong Acad Agr Sci, Inst Vet Med, Guangzhou 510642, Guangdong, Peoples R China

来源：

JOURNAL OF ANIMAL AND VETERINARY ADVANCES | 2012年 / 11卷 / 21期

关键词：

Riemerella anatipestifer; outer membrane phospholipase A; methyl arachidonyl fluorophosphonate; protein; database; PHOSPHOLIPASE-A; MOLECULAR CHARACTERIZATION; VIRULENCE GENES; IDENTIFICATION; DUCKS; COLONIZATION; SEROTYPES; COLI; PLDA;

D O I：

暂无

中图分类号：

S85 [动物医学（兽医学）];

学科分类号：

0906 ;

摘要：

A gene (pld4) encoding a 33.0 kDa protein. with significant homology to the Escherichia coli outer membrane phospholipase A was identified from Riemerella anatipestifer genome database. The results of this study revealed that this gene encoded an Outer Membrane Phospholipase A (OMPLA) in Riemerella anatipestifer. The recombinant ONEPLA protein. was expressed and its general biochemical features were also, determined. Methyl Arachidonyl Fluorophosphonate (MAFP) could specifically inhibit the OMPLA activity. These observations suggest that OMPLA could be exploited as a drug target in the bacteria and MAFP may serve as a lead compound for drug discovery against R. anatipestifer.

引用

页码：4073 / 4078

页数：6

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