Cloning and characterization of a nonhemolytic phospholipase C gene from Burkholderia pseudomallei
Cloning and characterization of a nonhemolytic phospholipase C gene from Burkholderia pseudomallei
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DOI：
10.1128/jcm.37.11.3742-3745.1999
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发表时间：
1999-11-01
影响因子：
9.4
通讯作者：
Sarasombath, S
中科院分区：
文献类型：
--
作者：
Korbsrisate, S;Suwanasai, N;Sarasombath, S
从类鼻疽伯克霍尔德菌中克隆了一个磷脂酰胆碱水解磷脂酶C（PC-PLC）基因，序列分析表明该基因的开放阅读框编码700个氨基酸，信号肽为34个氨基酸。当切割时，产生分泌的73-kDa成熟蛋白。推导的氨基酸序列与铜绿假单胞菌的非溶血性PLC具有48%的相似性，表达的PC-PLC是热稳定的，对绵羊红细胞是非溶血性的，并且在pH 2和8之间具有活性。类鼻疽患者血清的Western印迹分析表明，他们产生了针对这种PC-PLC蛋白的免疫球蛋白M抗体。
We cloned and characterized a phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC) gene from Burkholderia pseudomallei, DNA sequence analysis of the gene indicated an open reading frame coding for 700 amino acids with a 34-amino-acid signal peptide. When cleaved, this yields a secreted 73-kDa mature protein. The deduced amino acid sequence exhibited 48% similarity to that of a nonhemolytic PLC from Pseudomonas aeruginosa, The expressed PC-PLC was heat stable, nonhemolytic for sheep erythrocytes, and active between pH 2 and 8. Western blot analysis with sera from melioidosis patients indicated that they produced immunoglobulin M antibodies against this PC-PLC protein.