Abstract
We used surface plasmon resonance to study the binding of a set of soluble mouse I-E class II major histocompatibility molecules, each occupied by a different single peptide, to the staphylococcal enterotoxin superantigens, SEA and SEB. The rates of association and dissociation to SEA varied greatly depending on the I-E-bound peptide. By contrast, binding to SEB yielded fast association and dissociation rates, which were relatively peptide independent. The results also indicated nonoverlapping binding sites for SEB and SEA on class II and raised the possibility of enhanced SAg presentation to T cells by cross-linking of cell surface class II.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / immunology
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Base Sequence
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Binding Sites
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Enterotoxins / immunology
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Enterotoxins / metabolism*
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Epitope Mapping
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Histidine / chemistry
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Histocompatibility Antigens Class II / chemistry
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Histocompatibility Antigens Class II / metabolism*
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In Vitro Techniques
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Mice
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Models, Molecular
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / metabolism
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Protein Structure, Tertiary
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Recombinant Proteins
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Solubility
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Superantigens / metabolism*
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Zinc / physiology
Substances
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Antibodies, Monoclonal
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Enterotoxins
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Histocompatibility Antigens Class II
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I-E-antigen
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Peptides
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Recombinant Proteins
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Superantigens
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enterotoxin A, Staphylococcal
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enterotoxin B, staphylococcal
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Histidine
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Zinc