A solubilized T-cell receptor from a human leukemia cell line binds to a ligand in the absence of MHC products.
A human T cell alpha beta 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.
Fraser
J D
JD
Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.
Strominger
J L
JL
D000942:Antigens, Bacterial / Q000276:immunology*; D001426:Bacterial Proteins / Q000276:immunology / Q000378:metabolism*; D001665:Binding Sites; D002846:Chromatography, Affinity; D000939:Epitopes; D006649:Histocompatibility Antigens / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D008024:Ligands; D008285:Major Histocompatibility Complex; D011485:Protein Binding; D011948:Receptors, Antigen, T-Cell / Q000276:immunology / Q000378:metabolism*; D012995:Solubility; D013211:Staphylococcus aureus / Q000276:immunology; D014407:Tumor Cells, Cultured
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D000939:Epitopes; D006649:Histocompatibility Antigens; D008024:Ligands; D011948:Receptors, Antigen, T-Cell