The Salmonella Type III Secretion System Virulence Effector Forms a New Hexameric Chaperone Assembly for Export of Effector/Chaperone Complexes | Zendy

Chi-Lin Tsai | Zendy; Brianne J. Burkinshaw | Zendy; N.C.J. Strynadka | Zendy; John A. Tainer | Zendy

Open Access

The Salmonella Type III Secretion System Virulence Effector Forms a New Hexameric Chaperone Assembly for Export of Effector/Chaperone Complexes

Author(s) -

Chi-Lin Tsai,

Brianne J. Burkinshaw,

N.C.J. Strynadka,

John A. Tainer

Publication year - 2014

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.02524-14

Subject(s) - effector , chaperone (clinical) , biology , secretion , type three secretion system , virulence , cytosol , microbiology and biotechnology , salmonella , bacteria , biochemistry , genetics , gene , enzyme , medicine , pathology

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.

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