The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles

被引:269
作者
Mueller, CA
Broz, P
Müller, SA
Ringler, P
Erne-Brand, F
Sorg, I
Kuhn, M
Engel, A
Cornelis, GR
机构
[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
[2] Maurice E Muller Inst, CH-4056 Basel, Switzerland
关键词
D O I
10.1126/science.1118476
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Many pathogenic bacteria use injectisomes to deliver effector proteins into host cells through type III secretion. Injectisomes consist of a basal body embedded in the bacterial membranes and a needle. In Yersinia, translocation of effectors requires the YopB and YopD proteins, which form a pore in the target cell membrane, and the LcrV protein, which assists the assembly of the pore. Here we report that LcrV forms a distinct structure at the tip of the needle, the tip complex. This unique localization of LcrV may explain its crucial role in the translocation process and its efficacy as the main protective antigen against plague.
引用
收藏
页码:674 / 676
页数:3
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