Multivalent structure of an αβT cell receptor
Multivalent structure of an αβT cell receptor
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DOI：
10.1073/pnas.96.4.1547
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发表时间：
1999-02-16
影响因子：
11.1
通讯作者：
de la Hera, A
中科院分区：
文献类型：
--
作者：
Fernández-Miguel, G;Alarcón, B;de la Hera, A
在给定的TCR/CD 3复合物中是否存在一个或多个α β T细胞抗原受体（TCR）识别模块是免疫学中长期存在的争议。我们发现，来自共表达相当数量的两种不同TCR β链的转基因小鼠的T细胞在单个TCR/CD 3复合物中掺入至少两种α β TCR。双特异性α β TCR的证据通过免疫沉淀和免疫印迹获得，并通过荧光共振能量转移和共调节测定在活细胞表面上通过使用对TCR β可变区特异性的抗体来确认。这种（α β）（2）TCR/CD 3或更高级的复合物在离体或体外扩增后研究的T细胞中是明显的。许多人认为T细胞活化需要TCR通过其抗原/主要组织相容性复合物配体交联，但不是全部。多价（α-β）（2）TCR/CD 3复合物的化学计量的特定抗原/主要组织相容性复合物，CD 4或CD 8辅助受体和其他TCR的有序对接的影响进行了讨论。
Whether there is one or multiple alpha beta T cell antigen receptor (TCR) recognition modules in a given TCR/ CD3 complex is a long-standing controversy in immunology. We show that T cells from transgenic mice that coexpress comparable amounts of two distinct TCR beta chains incorporate at least two alpha beta TCRs in a single TCR/CD3 complex. Evidence for bispecific alpha beta TCRs was obtained by immunoprecipitation and immunoblotting and confirmed on the surface of living cells both by fluorescence resonance energy transfer and comodulation assays by using antibodies specific for TCR beta-variable regions. Such (alpha beta)(2)TCR/CD3 or higher-order complexes were evident in T cells studied either ex vivo or after expansion in vitro. T cell activation is thought by many, but not all, to require TCR cross-linking by its antigen/major histocompatibility complex ligand. The implications of a multivalent (alpha beta)(2)TCR/CD3 complex stoichiometry for the ordered docking of specific antigen/major histocompatibility complex, CD4, or CD8 coreceptors and additional TCRs are discussed.