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Complex high affinity interactions occur between MHCI and superantigens
Author(s) -
Chapes Stephen K.,
Herpich Angela R.
Publication year - 1998
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.64.5.587
Subject(s) - superantigen , biology , receptor , major histocompatibility complex , monoclonal antibody , microbiology and biotechnology , antibody , t cell receptor , mechanosensitive channels , biophysics , antigen , biochemistry , immunology , t cell , immune system , ion channel
Staphylococcal enterotoxins A and C1 (SEA or SEC1) bound to major histocompatibility‐I (MHCI) molecules with high affinity (binding constants ranging from 1.1 μM to 79 nM). SEA and SEC1 directly bound MHCI molecules that had been captured by monoclonal antibodies specific for H‐2K k , H‐2D k , or both. In addition, MHCI‐specific antibodies inhibited the binding of SEC1 to LM929 cells and SEA competitively inhibited SEC1 binding; indicating that the superantigens bound to MHCI on the cell surface. The affinity and number of superantigen binding sites differed depending on whether MHCI was expressed in the membrane of LM929 cells or whether it was captured. These data support the hypothesis that MHCI molecules can serve as superantigen receptors. J. Leukoc. Biol. 64:587–594; 1998.