This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kubori, T.
Right arrow Articles by Galán, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kubori, T.
Right arrow Articles by Galán, J. E.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2002, p. 4699-4708, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4699-4708.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Salmonella Type III Secretion-Associated Protein InvE Controls Translocation of Effector Proteins into Host Cells

Tomoko Kubori and Jorge E. Galán*

Section of Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut 06536

Received 21 March 2002/ Accepted 5 June 2002

Salmonella enterica encodes a type III secretion system (TTSS) within a pathogenicity island located at centisome 63 (SPI-1), which is essential for its pathogenicity. This system mediates the transfer of a battery of bacterial proteins into the host cell with the capacity to modulate cellular functions. The transfer process is dependent on the function of protein translocases SipB, SipC, and SipD. We report here that Salmonella protein InvE, which is also encoded within SPI-1, is essential for the translocation of bacterial proteins into host cells. An S. enterica serovar Typhimurium mutant carrying a loss-of-function mutation in invE shows reduced secretion of SipB, SipC, and SipD while exhibiting increased secretion of other TTSS effector proteins. We also demonstrate that InvE interacts with a protein complex formed by SipB, SipC, and their cognate chaperone, SicA. We propose that InvE controls protein translocation by regulating the function of the Sip protein translocases.

* Corresponding author. Mailing address: Section of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06536. Phone: (203) 737-2404. Fax: (203) 737-2630. E-mail: jorge.galan{at}yale.edu.

Journal of Bacteriology, September 2002, p. 4699-4708, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4699-4708.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Miki, T., Shibagaki, Y., Danbara, H., Okada, N. (2009). Functional Characterization of SsaE, a Novel Chaperone Protein of the Type III Secretion System Encoded by Salmonella Pathogenicity Island 2. J. Bacteriol. 191: 6843-6854 [Abstract] [Full Text]  
  • Desin, T. S., Lam, P.-K. S., Koch, B., Mickael, C., Berberov, E., Wisner, A. L. S., Townsend, H. G. G., Potter, A. A., Koster, W. (2009). Salmonella enterica Serovar Enteritidis Pathogenicity Island 1 Is Not Essential for but Facilitates Rapid Systemic Spread in Chickens. Infect. Immun. 77: 2866-2875 [Abstract] [Full Text]  
  • Kim, H. G., Kim, B. H., Kim, J. S., Eom, J. S., Bang, I.-S., Bang, S. H., Lee, I. S., Park, Y. K. (2008). N-terminal residues of SipB are required for its surface localization on Salmonella enterica serovar Typhimurium. Microbiology 154: 207-216 [Abstract] [Full Text]  
  • Kim, B. H., Kim, H. G., Kim, J. S., Jang, J. I., Park, Y. K. (2007). Analysis of functional domains present in the N-terminus of the SipB protein. Microbiology 153: 2998-3008 [Abstract] [Full Text]  
  • Fu, Z. Q., Guo, M., Alfano, J. R. (2006). Pseudomonas syringae HrpJ Is a Type III Secreted Protein That Is Required for Plant Pathogenesis, Injection of Effectors, and Secretion of the HrpZ1 Harpin.. J. Bacteriol. 188: 6060-6069 [Abstract] [Full Text]  
  • Kenjale, R., Wilson, J., Zenk, S. F., Saurya, S., Picking, W. L., Picking, W. D., Blocker, A. (2005). The Needle Component of the Type III Secreton of Shigella Regulates the Activity of the Secretion Apparatus. J. Biol. Chem. 280: 42929-42937 [Abstract] [Full Text]  
  • Ideses, D., Gophna, U., Paitan, Y., Chaudhuri, R. R., Pallen, M. J., Ron, E. Z. (2005). A Degenerate Type III Secretion System from Septicemic Escherichia coli Contributes to Pathogenesis. J. Bacteriol. 187: 8164-8171 [Abstract] [Full Text]  
  • Deng, W., Li, Y., Hardwidge, P. R., Frey, E. A., Pfuetzner, R. A., Lee, S., Gruenheid, S., Strynakda, N. C. J., Puente, J. L., Finlay, B. B. (2005). Regulation of Type III Secretion Hierarchy of Translocators and Effectors in Attaching and Effacing Bacterial Pathogens. Infect. Immun. 73: 2135-2146 [Abstract] [Full Text]  
  • Dale, C., Jones, T., Pontes, M. (2005). Degenerative Evolution and Functional Diversification of Type-III Secretion Systems in the Insect Endosymbiont Sodalis glossinidius. Mol Biol Evol 22: 758-766 [Abstract] [Full Text]  
  • Ghosh, P. (2004). Process of Protein Transport by the Type III Secretion System. Microbiol. Mol. Biol. Rev. 68: 771-795 [Abstract] [Full Text]  
  • Akeda, Y., Galan, J. E. (2004). Genetic Analysis of the Salmonella enterica Type III Secretion-Associated ATPase InvC Defines Discrete Functional Domains. J. Bacteriol. 186: 2402-2412 [Abstract] [Full Text]  
  • Deng, W., Puente, J. L., Gruenheid, S., Li, Y., Vallance, B. A., Vazquez, A., Barba, J., Ibarra, J. A., O'Donnell, P., Metalnikov, P., Ashman, K., Lee, S., Goode, D., Pawson, T., Finlay, B. B. (2004). Dissecting virulence: Systematic and functional analyses of a pathogenicity island. Proc. Natl. Acad. Sci. USA 101: 3597-3602 [Abstract] [Full Text]  
  • Day, J. B., Lee, C. A. (2003). Secretion of the orgC Gene Product by Salmonella enterica Serovar Typhimurium. Infect. Immun. 71: 6680-6685 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»