Major histocompatibility complex recognition by immune receptors: differences among T cell receptor versus antibody interactions with the VSV8/H-2Kb complex.
Major histocompatibility complex recognition by immune receptors: differences among T cell receptor versus antibody interactions with the VSV8/H-2Kb complex.
复制标题
免疫受体对主要组织相容性复合物的识别：T 细胞受体与抗体与 VSV8/H-2Kb 复合物相互作用之间的差异。
DOI：
10.1002/eji.1830270134
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Chang,HC
中科院分区：
文献类型：
--
作者：
Witte,T;Smolyar,A;Spoerl,R;Goyarts,EC;Nathenson,SG;Reinherz,EL;Chang,HC
通过突变分析绘制了VSV 8/Kb复合物的表面残基，这些残基对于N15和N26 αβ T细胞受体（TCR）的识别至关重要，并相互比较，并与充分表征的Kb特异性单克隆抗体（mAb）的表位进行比较。免疫受体识别的三个特征出现了。首先，VSV 8/Kbare上两种TCR的足迹相似，位点之间重叠超过80%。鉴于14个表面暴露的VSV 8/Kb残基中鉴定为TCR相互作用关键的仅8个是共同的，N15和N26相互作用的化学基础仍然是不同的。第二，同源肽是TCR识别的主要焦点：在三个暴露侧链中的任何一个（在p1、p4或p6）处的突变消除了两个TCR的相互作用，如通过功能性T细胞活化所测量的。第三，与TCR相反，mAb与α1和/或α2螺旋外周上的离散片段结合而没有取向限制。这些发现表明，与可溶性抗体不同，相对细胞（即TCR-肽/MHC，CD 8-MHC）上的表面膜受体-配体相互作用限制了TCR在免疫识别过程中的取向自由度。
The surface residues of the VSV8/Kbcomplex important for recognition by N15 and N26 αβ T cell receptors (TCR) were mapped by mutational analysis and compared to each other and with epitopes of well‐characterized Kbspecific monoclonal antibodies (mAb). Three features of immune receptor recognition emerge. First, the footprints of the two TCR on VSV8/Kbare similar with more than 80% overlap between sites. Given that only 8 of 14 surface exposed VSV8/Kbresidues identified as critical for TCR interaction are in common, the chemical basis of the N15 and N26 interactions is nevertheless distinct. Second, the cognate peptide is a major focus of TCR recognition: mutation at any of the three exposed side chains (at p1, p4 or p6) abrogates interaction of both TCR as measured by functional T cell activation. Third, in contrast to TCR, mAb bind to discrete segments on the periphery of the α1 and/or α2 helices without orientational restriction. These findings suggest that unlike soluble antibodies, surface membrane receptor‐ligand interactions on opposing cells (i.e.TCR‐peptide/MHC, CD8‐MHC) limit the orientational freedom of the TCR in the immune recognition process.