Sequences in both class II major histocompatibility complex alpha and beta chains contribute to the binding of the superantigen toxic shock syndrome toxin 1. (original) (raw)
Article| May 01 1992
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
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Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Search for other works by this author on:
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Search for other works by this author on:
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Search for other works by this author on:
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Search for other works by this author on:
N S Braunstein, D A Weber, X C Wang, E O Long, D Karp
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Online ISSN: 1540-9538
Print ISSN: 0022-1007
J Exp Med (1992) 175 (5): 1301–1305.
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.
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