Subcellular targeting of Salmonella virulence proteins by host-mediated S-palmitoylation.
Subcellular targeting of Salmonella virulence proteins by host-mediated S-palmitoylation.
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DOI：
10.1016/j.chom.2011.06.003
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发表时间：
2011-07-21
影响因子：
30.3
通讯作者：
Galán JE
中科院分区：
文献类型：
--
作者：
Hicks SW;Charron G;Hang HC;Galán JE
几种致病菌利用III型分泌系统（T3SS）向宿主细胞传递具有调节多种细胞途径能力的细菌毒力蛋白。一旦进入宿主细胞，细菌效应物准确定位到特定位置对其正常发挥作用至关重要。然而，人们对这些毒力效应物到达亚细胞目的地的机制知之甚少。在这里，我们发现沙门氏菌T3SS效应蛋白SspH2和SseI定位于宿主细胞的质膜，这一过程依赖于其n端区域内保守的半胱氨酸残基的s -棕榈酰化。我们还表明，效应蛋白脂化是由宿主细胞棕榈酰转移酶的一个特定亚群介导的，脂化对它们的功能至关重要。本研究描述了病原体利用宿主细胞机制正确靶向其毒力因子的显著机制。
Several pathogenic bacteria utilize type III secretion systems (T3SS) to deliver into host cells bacterial virulence proteins with the capacity to modulate a variety of cellular pathways. Once delivered into host cells, the accurate targeting of bacterial effectors to specific locations is critical for their proper function. However, little is known about the mechanisms these virulence effectors use to reach their subcellular destination. Here, we show that the Salmonella T3SS effector proteins SspH2 and SseI are localized to the plasma membrane of host cells, a process dependent on S-palmitoylation of a conserved cysteine residue within their N-terminal domains. We also show that effector protein lipidation is mediated by a specific subset of host-cell palmitoyltransferases and that lipidation is critical for their function. This study describes a remarkable mechanism by which a pathogen exploits host-cell machinery to properly target its virulence factors.
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影响因子：
3.9
作者：
Greaves, Jennifer;Chamberlain, Luke H.
通讯作者：
Chamberlain, Luke H.
影响因子：
4.5
作者：
Hou, Haitong;Peter, Arun T. John;Ungermann, Christian
通讯作者：
Ungermann, Christian
DOI：
10.1074/jbc.m900519200
发表时间：
2009-06-05
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Dowen RH;Engel JL;Shao F;Ecker JR;Dixon JE
通讯作者：
Dixon JE
影响因子：
3.4
作者：
Ibarra JA;Steele-Mortimer O
通讯作者：
Steele-Mortimer O
影响因子：
3.2
作者：
GUZMAN, LM;BELIN, D;BECKWITH, J
通讯作者：
BECKWITH, J