A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type III secretion

被引:16
作者
Allen-Vercoe, E [1 ]
Toh, MCW [1 ]
Waddell, B [1 ]
Ho, H [1 ]
DeVinney, R [1 ]
机构
[1] Univ Calgary, Hlth Sci Ctr, Dept Microbiol & Infect Dis, Calgary, AB T2N 4N1, Canada
基金
加拿大健康研究院;
关键词
Tir; host-pathogen interactions; enterohemorrhagic Escherichia coli; protein-protein interaction; type III secretion;
D O I
10.1016/j.femsle.2004.12.027
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The type III secreted protein Tir from Enterohemorrhagic Escherichia coli (EHEC O157:H7) plays a central role in adherence and pedestal formation during infection. Little is known about how Tir domains outside of the amino-terminus contribute to efficient Tir secretion and translocation. We found a 6 amino acid (519-524) carboxy-terminal region which was required for efficient Tir secretion and translocation. Interestingly, EHEC O157:H7 TirDelta519-524 was efficiently secreted when expressed in the related pathogen enteropathogenic E. coli. These data suggest that this region may play a role in maintaining EHEC O157:H7 Tir in a secretion-competent conformation. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:355 / 364
页数:10
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