Siliciano R F, Hemesath T J, Pratt J C, Dintzis R Z, Dintzis H M, Acuto O, Shin H S, Reinherz E L
Cell. 1986 Oct 24;47(2):161-71. doi: 10.1016/0092-8674(86)90439-3.
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.
通过流式细胞术和亲和层析法检测了名义抗原与对异硫氰酸荧光素（FL）具有特异性的MHC限制性人T细胞克隆上的Tiα-β异二聚体的结合。FL-Ti相互作用具有生理意义，因为在没有特异性MHC识别的情况下，交联的FL阵列可诱导T细胞活化。需要高抗原价才能实现与细胞的稳定结合及随后的活化，这与估计的Ti-FL缔合常数小于3×10⁵ l/mol一致。除了提供直接证据证明Tiα-β异二聚体是抗原受体外，这些数据还表明至少一些MHC限制性克隆的Ti分子上存在名义抗原结合位点。
