IDENTIFICATION OF PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C ACTIVITY IN LISTERIA-MONOCYTOGENES - A NOVEL TYPE OF VIRULENCE FACTOR

被引：168
|
作者：
MENGAUD, J
BRAUNBRETON, C
COSSART, P
机构：
[1] INST PASTEUR,UNITE GENIE MICROBIOL,25 RUE DR ROUX,F-75724 PARIS 15,FRANCE
[2] INST PASTEUR,UNITE PARASITOL EXPTL,F-75724 PARIS 15,FRANCE
来源：
MOLECULAR MICROBIOLOGY | 1991年 / 5卷 / 02期
关键词：
D O I：
10.1111/j.1365-2958.1991.tb02118.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A phospholipase C which cleaves phosphatidylinositol and glycosylphosphatidylinositol (GPI) anchors was identified in Listeria monocytogenes. This 36 kDa protein is encoded by the gene plcA, and is homologous to the Bacillus cereus, Bacillus thuringiensis and eukaryotic phosphatidylinositol-specific phospholipases C (PI-PLC). Expression of the plcA gene in Escherichia coli correlates with the appearance of PI-PLC activity in the cells. In Listeria monocytogenes, the activity is secreted to the culture medium. PI-PLC activity was only found in the two pathogenic species of the genus Listeria, namely L. monocytogenes and L. ivanolii. PI-PLC activity was lost and virulence decreased when the plcA gene was disrupted in the chromosome. This suggests that the PI-PLC of L. monocytogenes might be involved in virulence.
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页码：367 / 372
页数：6
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