Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Logo for

Science 330 (6002): 390-393

Copyright © 2010 by the American Association for the Advancement of Science

Salmonella Pathogenesis and Processing of Secreted Effectors by Caspase-3

C. V. Srikanth,1,2,* Daniel M. Wall,1,3,* Ana Maldonado-Contreras,2 Hai Ning Shi,1 Daoguo Zhou,4 Zachary Demma,2 Karen L. Mumy,1,2 Beth A. McCormick1,2,{dagger}

Abstract: The enteric pathogen Salmonella enterica serovar Typhimurium causes food poisoning resulting in gastroenteritis. The S. Typhimurium effector Salmonella invasion protein A (SipA) promotes gastroenteritis by functional motifs that trigger either mechanisms of inflammation or bacterial entry. During infection of intestinal epithelial cells, SipA was found to be responsible for the early activation of caspase-3, an enzyme that is required for SipA cleavage at a specific recognition motif that divided the protein into its two functional domains and activated SipA in a manner necessary for pathogenicity. Other caspase-3 cleavage sites identified in S. Typhimurium appeared to be restricted to secreted effector proteins, which indicates that this may be a general strategy used by this pathogen for processing of its secreted effectors.

1 Department of Pediatric Gastroenterology and Nutrition, Harvard Medical School and Massachusetts General Hospital, Boston, MA 02129, USA.
2 Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.
3 Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
4 Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: Beth.McCormick{at}umassmed.edu


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structure of an SspH1-PKN1 Complex Reveals the Basis for Host Substrate Recognition and Mechanism of Activation for a Bacterial E3 Ubiquitin Ligase.
A. F. A. Keszei, X. Tang, C. McCormick, E. Zeqiraj, J. R. Rohde, M. Tyers, and F. Sicheri (2014)
Mol. Cell. Biol. 34, 362-373
   Abstract »    Full Text »    PDF »
The Inside Story of Shigella Invasion of Intestinal Epithelial Cells.
N. Carayol and G. Tran Van Nhieu (2013)
Cold Spring Harb Perspect Med 3, a016717
   Abstract »    Full Text »    PDF »
The Actin-Polymerizing Activity of SipA Is Not Essential for Salmonella enterica Serovar Typhimurium-Induced Mucosal Inflammation.
D. Li, X. Wang, L. Wang, and D. Zhou (2013)
Infect. Immun. 81, 1541-1549
   Abstract »    Full Text »    PDF »
Bacterial Escape Artists Set Afire.
M. Cemma and J. H. Brumell (2013)
Science 339, 912-913
   Abstract »    Full Text »    PDF »
The Salmonella Typhimurium effector SteC inhibits Cdc42-mediated signaling through binding to the exchange factor Cdc24 in Saccharomyces cerevisiae.
P. Fernandez-Pinar, A. Aleman, J. Sondek, H. G. Dohlman, M. Molina, and H. Martin (2012)
Mol. Biol. Cell 23, 4430-4443
   Abstract »    Full Text »    PDF »
Infection with Mycobacterium avium subsp. paratuberculosis Results in Rapid Interleukin-1{beta} Release and Macrophage Transepithelial Migration.
E. A. Lamont, S. M. O'Grady, W. C. Davis, T. Eckstein, and S. Sreevatsan (2012)
Infect. Immun. 80, 3225-3235
   Abstract »    Full Text »    PDF »
Functions of the Salmonella pathogenicity island 2 (SPI-2) type III secretion system effectors.
R. Figueira and D. W. Holden (2012)
Microbiology 158, 1147-1161
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882