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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1989-11-9
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pubmed:abstractText |
Staphylococcal enterotoxins (SE) activate human T cells in vitro. This requires the presence of Ia+ accessory cells but does not require processing of the toxin by the accessory cell. We and others have recently demonstrated direct binding of SE to human MHC class II molecules. In this study, we have compared in detail the ability of class II molecules to bind two SE, toxic shock syndrome toxin-1 (TSST-1) and SEB. Scatchard analysis of equilibrium binding data indicate that SEB binds to Ia+ human cell lines with a 10-fold lower affinity than TSST-1. Likewise, SEB precipitates HLA-DR alpha- and beta-chains from detergent lysates of Ia+ cells less efficiently than TSST-1. The binding of TSST-1 and SEB to transfected L cells expressing HLA-DR and HLA-DQ gene products was differentially inhibited by anti-HLA-DR mAb. There was virtually no cross-inhibition of TSST-1 and SEB in competitive binding assays. We conclude that TSST-1 and SEB bind to two MHC class II sites which can be distinguished by their relative accessibility to blocking by anti-class II mAb and heterologous toxin.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQ Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Guanylate Cyclase-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Superantigens,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin B, staphylococcal,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin F, Staphylococcal,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2583-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2551962-Antibodies, Monoclonal,
pubmed-meshheading:2551962-Bacterial Toxins,
pubmed-meshheading:2551962-Binding, Competitive,
pubmed-meshheading:2551962-Chromatography, Affinity,
pubmed-meshheading:2551962-Cross Reactions,
pubmed-meshheading:2551962-Enterotoxins,
pubmed-meshheading:2551962-Guanylate Cyclase,
pubmed-meshheading:2551962-HLA-DQ Antigens,
pubmed-meshheading:2551962-HLA-DR Antigens,
pubmed-meshheading:2551962-Humans,
pubmed-meshheading:2551962-Kinetics,
pubmed-meshheading:2551962-L Cells (Cell Line),
pubmed-meshheading:2551962-Receptors, Cell Surface,
pubmed-meshheading:2551962-Receptors, Guanylate Cyclase-Coupled,
pubmed-meshheading:2551962-Receptors, Peptide,
pubmed-meshheading:2551962-Staphylococcus aureus,
pubmed-meshheading:2551962-Superantigens,
pubmed-meshheading:2551962-Transfection
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pubmed:year |
1989
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pubmed:articleTitle |
Staphylococcal enterotoxin B and toxic shock syndrome toxin-1 bind to distinct sites on HLA-DR and HLA-DQ molecules.
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pubmed:affiliation |
Division of Allergy and Immunology, Children's Hospital, Boston, MA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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