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 Shupp, J. W.
Right arrow Articles by Pontzer, C. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shupp, J. W.
Right arrow Articles by Pontzer, C. H.

 Previous Article  |  Next Article 

Infection and Immunity, April 2002, p. 2178-2186, Vol. 70, No. 4
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.4.2178-2186.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification of a Transcytosis Epitope on Staphylococcal Enterotoxins

Jeffrey W. Shupp,1 Marti Jett,2 and Carol H. Pontzer1*

Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742 ,1 Division of Pathology, Walter Reed Army Institute of Research, Silver Spring, Maryland 209102

Received 29 October 2001/ Returned for modification 7 December 2001/ Accepted 16 January 2002

Staphylococcal enterotoxins (SE) are exoproteins produced by Staphylococcus aureus that act as superantigens and have been implicated as a leading cause of food-borne disease and toxic shock. Little is known about how these molecules penetrate the gut lining and gain access to both local and systemic immune tissues. To model movement in vitro of staphylococcal enterotoxins, we have employed a monolayer system composed of crypt-like human colonic T-84 cells. SEB and SEA showed comparable dose-dependent transcytosis in vitro, while toxic shock syndrome toxin (TSST-1) exhibited increased movement at lower doses. Synthetic peptides corresponding to specific regions of the SEB molecule were tested in vitro to identify the domain of the protein involved in the transcytosis of SE. A toxin peptide of particular interest contains the amino acid sequence KKKVTAQELD, which is highly conserved across all SE. At a toxin-to-peptide ratio of 1:10, movement of SEB across the monolayers was reduced by 85%. Antisera made against the SEB peptide recognized native SEB and also inhibited SEB transcytosis. Finally, the conserved 10-amino-acid peptide inhibited transcytosis of multiple staphylococcal enterotoxins, SEA, SEE, and TSST-1. These data demonstrate that this region of the staphylococcal enterotoxins plays a distinct role in toxin movement across epithelial cells. It has implications for the prevention of staphylococcal enterotoxin-mediated disease by design of a peptide vaccine that could reduce systemic exposure to oral or inhaled superantigens. Since the sequence identified is highly conserved, it allows for a single epitope blocking the transcytosis of multiple SE.

* Corresponding author. Mailing address: Dept. Cell Biol. & Molec. Gen., Bldg. 231, University of Maryland, College Park, MD 20742. Phone: (301) 405-5472. Fax: (301) 314-9489. E-mail: cp75{at}umail.umd.edu.

Editor: J. T. Barbieri

Infection and Immunity, April 2002, p. 2178-2186, Vol. 70, No. 4
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.4.2178-2186.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chatterjee, S., Neill, R., Shupp, J. W., Hammamieh, R., Ionin, B., Jett, M. (2007). Identification of Staphylococcal Enterotoxin B Domains Involved in Binding to Cultured Human Kidney Proximal Tubular Cells: Imparting Proliferation and Death. Exp. Biol. Med. 232: 1142-1151 [Abstract] [Full Text]  
  • Pinchuk, I. V., Beswick, E. J., Saada, J. I., Suarez, G., Winston, J., Mifflin, R. C., Di Mari, J. F., Powell, D. W., Reyes, V. E. (2007). Monocyte Chemoattractant Protein-1 Production by Intestinal Myofibroblasts in Response to Staphylococcal Enterotoxin A: Relevance to Staphylococcal Enterotoxigenic Disease. J. Immunol. 178: 8097-8106 [Abstract] [Full Text]  
  • Peterson, M. L., Ault, K., Kremer, M. J., Klingelhutz, A. J., Davis, C. C., Squier, C. A., Schlievert, P. M. (2005). The Innate Immune System Is Activated by Stimulation of Vaginal Epithelial Cells with Staphylococcus aureus and Toxic Shock Syndrome Toxin 1. Infect. Immun. 73: 2164-2174 [Abstract] [Full Text]  
  • van Gessel, Y. A., Mani, S., Bi, S., Hammamieh, R., Shupp, J. W., Das, R., Coleman, G. D., Jett, M. (2004). Functional Piglet Model for the Clinical Syndrome and Postmortem Findings Induced by Staphylococcal Enterotoxin B. Exp. Biol. Med. 229: 1061-1071 [Abstract] [Full Text]  
  • Musch, M. W., Petrof, E. O., Kojima, K., Ren, H., McKay, D. M., Chang, E. B. (2004). Bacterial Superantigen-Treated Intestinal Epithelial Cells Upregulate Heat Shock Proteins 25 and 72 and Are Resistant to Oxidant Cytotoxicity. Infect. Immun. 72: 3187-3194 [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»