Secretion of the Escherichia coli K-12 sheA hemolysin is independent of its cytolytic activity

被引:18
作者
del Castillo, FJ [1 ]
Moreno, F [1 ]
del Castillo, I [1 ]
机构
[1] Hosp Ramon y Cajal, Mol Genet Unit, E-28034 Madrid, Spain
关键词
SheA hemolysin; bacterial protein secretion; beta-lactamase gene fusion; outer membrane vesicle;
D O I
10.1016/S0378-1097(01)00413-X
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The Escherichia coli K-12 sheA gene encodes a pore-forming hemolysin that is secreted to the medium by a hitherto unidentified mechanism. To study SheA secretion, we constructed fusions between SheA and the mature form of the periplasmic enzyme beta -lactamase, and performed site-directed mutagenesis on these constructs. The SheA-Bla and Bla-SheA hybrid proteins displayed hemolytic activity and were efficiently exported to the extracellular medium. Our results with mutant hybrid proteins show that secretion of SheA is independent of its cytolytic activity, that secretion is paralleled by a transient leakage of periplasmic contents to the extracellular medium, and that deletion of the 11 C-terminal residues, of SheA has no effect on its secretion and cytolytic activity. (C) 2001 Federation of European Microbiological Societies, Published by Elsevier Science BN. All rights reserved.
引用
收藏
页码:281 / 285
页数:5
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