Sequences in both class II major histocompatibility complex alpha and beta chains contribute to the binding of the superantigen toxic shock syndrome toxin 1.
Class II major histocompatibility complex (MHC) molecules present peptides derived from processed antigen to antigen-specific CD4-positive T cells. In addition, class II molecules bind with high affinity another class of antigens, termed superantigens. T cell stimulation by superantigens depends almost exclusively on the V beta segment expressed by the T cell receptor (TCR). Mapping of the superantigen binding site on class II molecules should provide valuable information on how MHC and TCR molecules interact. Recombinant mouse I-A class II molecules expressed on transfected L cells were analyzed for their ability to bind the toxic shock syndrome toxin 1. Polymorphic residues in the alpha helices of both the alpha and beta chains of I-A contributed to quantitative toxin binding, suggesting that the toxin binds to either a combinatorial or a conformational site on class II MHC molecules.
Braunstein
N S
NS
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Weber
D A
DA
Wang
X C
XC
Long
E O
EO
Karp
D
D
D000818:Animals; D001427:Bacterial Toxins; D002460:Cell Line; D004768:Enterotoxins / Q000276:immunology*; D000949:Histocompatibility Antigens Class II / Q000235:genetics / Q000378:metabolism*; D007739:L Cells; D051379:Mice; D011994:Recombinant Proteins / Q000276:immunology; D018089:Superantigens; D014162:Transfection
D001427:Bacterial Toxins; D004768:Enterotoxins; D000949:Histocompatibility Antigens Class II; D011994:Recombinant Proteins; D018089:Superantigens; C030107:enterotoxin F, Staphylococcal