Direct evidence for the existence of nominal antigen binding sites on T cell surface Ti alpha-beta heterodimers of MHC-restricted T cell clones.
Siliciano RF., Hemesath TJ., Pratt JC., Dintzis RZ., Dintzis HM., Acuto O., Shin HS., Reinherz EL.
The binding of nominal antigen to Ti alpha-beta heterodimers on MHC-restricted human T cell clones specific for fluorescein-5-isothiocyanate (FL) was detected by flow cytometry and affinity chromatography. The FL-Ti interaction is of physiologic significance, since T cell activation is induced by cross-linked arrays of FL in the absence of the specific MHC recognition. High antigen valence is required to achieve stable binding to cells and subsequent activation, which is consistent with estimated Ti-FL association constants of less than 3 X 10(5) l/mol. In addition to providing direct evidence that the Ti alpha-beta heterodimer is the receptor for antigen, these data suggest that nominal antigen binding sites exist on the Ti molecules of at least some MHC-restricted clones.