The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes

Chi Lin Tsai; Brianne J. Burkinshaw; Natalie C.J. Strynadka; John A. Tainer

doi:10.1128/JB.02524-14

The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes

Chi Lin Tsai, Brianne J. Burkinshaw, Natalie C.J. Strynadka, John A. Tainer

Research output: Contribution to journal › Comment/debate › peer-review

11 Scopus citations

Abstract

Bacteria hijack eukaryotic cells by injecting virulence effectors into host cytosol with a type III secretion system (T3SS). Effectors are targeted with their cognate chaperones to hexameric T3SS ATPase at the bacterial membrane's cytosolic face. In this issue of the Journal of Bacteriology, Roblin et al. (P. Roblin, F. Dewitte, V. Villeret, E. G. Biondi, and C. Bompard, J Bacteriol 197:688-698, 2015, http://dx.doi.org/10.1128/JB.02294-14) show that the T3SS chaperone SigE of Salmonella can form hexameric rings rather than dimers when bound to its cognate effector, SopB, implying a novel multimeric association for chaperone/effector complexes with their ATPase.

Original language	English (US)
Pages (from-to)	672-675
Number of pages	4
Journal	Journal of bacteriology
Volume	197
Issue number	4
DOIs	https://doi.org/10.1128/JB.02524-14
State	Published - 2015
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Molecular Biology

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10.1128/JB.02524-14

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abstract = "Bacteria hijack eukaryotic cells by injecting virulence effectors into host cytosol with a type III secretion system (T3SS). Effectors are targeted with their cognate chaperones to hexameric T3SS ATPase at the bacterial membrane's cytosolic face. In this issue of the Journal of Bacteriology, Roblin et al. (P. Roblin, F. Dewitte, V. Villeret, E. G. Biondi, and C. Bompard, J Bacteriol 197:688-698, 2015, http://dx.doi.org/10.1128/JB.02294-14) show that the T3SS chaperone SigE of Salmonella can form hexameric rings rather than dimers when bound to its cognate effector, SopB, implying a novel multimeric association for chaperone/effector complexes with their ATPase.",

author = "Tsai, {Chi Lin} and Burkinshaw, {Brianne J.} and Strynadka, {Natalie C.J.} and Tainer, {John A.}",

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AU - Strynadka, Natalie C.J.

AU - Tainer, John A.

PY - 2015

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The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes

Abstract

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