The recognition of the nonclassical major histocompatibility complex (MHC) class I molecule, T10, by the gammadelta T cell, G8.
Recent studies have shown that many nonclassical major histocompatibility complex (MHC) (class 1b) molecules have distinct antigen-binding capabilities, including the binding of nonpeptide moieties and the binding of peptides that are different from those bound to classical MHC molecules. Here, we show that one of the H-2T region-encoded molecules, T10, when produced in Escherichia coli, can be folded in vitro with beta2-microglobulin (beta2m) to form a stable heterodimer in the absence of peptide or nonpeptide moieties. This heterodimer can be recognized by specific antibodies and is stimulatory to the gammadelta T cell clone, G8. Circular dichroism analysis indicates that T10/beta2m has structural features distinct from those of classical MHC class I molecules. These results suggest a new way for MHC-like molecules to adopt a peptide-free structure and to function in the immune system.
Crowley
M P
MP
Program in Immunology, Stanford University School of Medicine, California 94305, USA.
Reich
Z
Z
Mavaddat
N
N
Altman
J D
JD
Chien
Y
Y
D002999:Clone Cells; D019281:Dimerization; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000276:immunology*; D008285:Major Histocompatibility Complex; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D016692:Receptors, Antigen, T-Cell, gamma-delta / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology; D016176:T-Lymphocyte Subsets / Q000276:immunology*; D001613:beta 2-Microglobulin / Q000276:immunology*
D015395:Histocompatibility Antigens Class I; D016692:Receptors, Antigen, T-Cell, gamma-delta; D011994:Recombinant Proteins; D001613:beta 2-Microglobulin