Tang X X, Ikegaki N, Danska J S, Heber-Katz E
Wistar Institute, Philadelphia, PA 19104, USA.
Mol Immunol. 1995 Jun;32(9):661-8. doi: 10.1016/0161-5890(95)00026-b.
We have attempted to elucidate the relative orientation of the T-cell receptor (TCR) to the major histocompatibility complex (MHC)-antigen complex during antigen recognition, using the T-cell response to B10.A (I-Ek) and B10.A(5R) (I-Eb) mice to the 1-23(H) peptide derived from glycoprotein D of the herpes simplex virus. The 1-23(H)-specific T-cells derived from both B10.A and B10.A(5R) mice use the same set of V alpha genes and a different array of V beta genes. The CDR1s of these TCR beta chains share residues at particular positions. The CDR2s of the TCR beta chains have a negative charge, which correlates with I-Eb reactivity and with the positively charged polymorphic residues residing at the C-terminal end of the alpha-helix of the I-Eb beta chain of the class II molecule. Taken together, the data suggest that the TCR beta chain interacts with both the alpha and beta chains of the MHC class II molecule, as does the TCR alpha chain.
我们试图通过利用T细胞对B10.A（I-Ek）和B10.A(5R)（I-Eb）小鼠针对单纯疱疹病毒糖蛋白D衍生的1-23(H)肽的反应，来阐明抗原识别过程中T细胞受体（TCR）与主要组织相容性复合体（MHC）-抗原复合体的相对取向。来自B10.A和B10.A(5R)小鼠的1-23(H)特异性T细胞使用同一组Vα基因和不同的Vβ基因阵列。这些TCRβ链的互补决定区1（CDR1）在特定位置共享残基。TCRβ链的互补决定区2（CDR2）带负电荷，这与I-Eb反应性以及与II类分子I-Ebβ链α螺旋C末端带正电荷的多态性残基相关。综合来看，数据表明TCRβ链与MHC II类分子的α链和β链相互作用，TCRα链也是如此。
