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

J Bacteriol. 2015 Feb 15;197(4):672-5. doi: 10.1128/JB.02524-14. Epub 2014 Dec 8.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism*
  • Salmonella typhimurium / metabolism*
  • Sigma Factor / chemistry*
  • Sigma Factor / metabolism*

Substances

  • Bacterial Proteins
  • Molecular Chaperones
  • Sigma Factor
  • SopB protein, Bacteria
  • sigE protein, Bacteria