A solubilized T-cell receptor from a human leukemia cell line binds to a ligand in the absence of MHC products |
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Authors: | John D Fraser Jack L Strominger |
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Institution: | (1) Harvard Medical School, Dana Farber Cancer Institute, 02115 Boston, MA, USA |
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Abstract: | A human T cell ![agr](/content/h722n47433654wm7/xxlarge945.gif) antigen receptor from the acute lymphoblastoid leukemia line HPB-ALL (also called HPB-MLT) binds and is precipitated in detergent solubilized form by an antigen present on the surface and secreted by several strains of the gram-positive bacterium Staphylococcus aureus. This binding is completely independent of major histocompatibility complex (MHC) antigens. Receptor/ligand binding is unique to this one cell line (i. e., clonotypic) and furthermore completely blocked by an idiotype-specific monoclonal antibody (mAb) to this receptor, but not by three different nonidiotype-specific mAbs. The nature of this interaction appears more similar to immunoglobulin/antigen binding than to T-cell receptor/antigen/MHC/accessory molecule interactions and would suggest that some T-cell receptors may not require MHC products to interact with antigen. |
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