The JI PBL Intereron Source
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lee, J. M.
Right arrow Articles by Watts, T. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lee, J. M.
Right arrow Articles by Watts, T. H.

The Journal of Immunology, Vol 145, Issue 10 3360-3366, Copyright © 1990 by American Association of Immunologists

ARTICLES

Binding of staphylococcal enterotoxin A to purified murine MHC class II molecules in supported lipid bilayers

JM Lee and TH Watts
Department of Immunology, University of Toronto, Ontario, Canada.

The staphylococcal enterotoxins are a family of bacterial toxins that are thought to exert their pathogenic effects by the massive activation of T lymphocytes to produce lymphokines. Activation of T cells by these toxins is dependent on MHC class II+ APC. Recent studies from a number of laboratories have implicated MHC class II proteins as the APC surface receptor for a number of the staphylococcal enterotoxins. The present report shows that staphylococcal enterotoxin A, (SEA) binds to the purified murine MHC class II molecule I-Ed reconstituted in supported planar membranes, indicating that no other cell surface proteins are required for SEA binding. The Kd for SEA binding to I-Ed was determined to be 3.5 +/- 1.6 x 10(-6) M. Specific binding of SEA to I-Ad was also observed, but the interaction was of significantly lower affinity. Binding of SEA to purified I-Ed was blocked by antibodies against both the alpha- and the beta-chain of the I-Ed molecule, but not by antibodies specific for an unrelated MHC class II protein. Binding of SEA to I-Ad was blocked by an A beta d but not by an A alpha d-specific antibody. Planar membranes containing only lipid and purified I-Ed molecules were sufficient for activation of a V beta 1 expressing T hybrid by SEA. The T cells responded to as few as 180 toxin molecules per T cell.


This article has been cited by other articles:


Home page
 GlycobiologyHome page
B. A Cobb and D. L Kasper
Characteristics of carbohydrate antigen binding to the presentation protein HLA-DR
Glycobiology, September 1, 2008; 18(9): 707 - 718.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
P. M. Lavoie, H. McGrath, N. H. Shoukry, P.-A. Cazenave, R.-P. Sekaly, and J. Thibodeau
Quantitative Relationship Between MHC Class II-Superantigen Complexes and the Balance of T Cell Activation Versus Death
J. Immunol., June 15, 2001; 166(12): 7229 - 7237.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
B. Ghumman, E. M. Bertram, and T. H. Watts
Chemical Chaperones Enhance Superantigen and Conventional Antigen Presentation by HLA-DM-Deficient as well as HLA-DM-Sufficient Antigen-Presenting Cells and Enhance IgG2a Production In Vivo
J. Immunol., October 1, 1998; 161(7): 3262 - 3270.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.