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Ligand-specific oligomerization of T-cell receptor molecules

机译：T细胞受体分子的配体特异性寡聚

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摘要

T cells initiate many immune responses through the interaction of their T-cell antigen receptors (TCR) with antigenic peptides bound to major histocompatibility complex (MHC) molecules. This interaction sends a biochemical signal into the T cell by a mechanism that is not clearly understood. We have used quasielastic light scattering (QELS) to show that, in the presence of MHC molecules bound to a full agonist peptide, TCR/peptide-MHC complexes oligomerize in solution to form supramolecular structures at concentrations near the dissociation constant of the binding reaction. The size of the oligomers is concentration dependent and is calculated to contain two to six ternary complexes for the concentrations tested here. This effect is specific as neither molecule forms oligomers by itself, nor were oligomers observed unless the correct peptide was bound to the MHC. These results provide direct evidence for models of T-cell signalling based on the specific assembly of multiple TCR/peptide-MHC complexes in which the degree of assembly determines the extent and qualitative nature of the transduced signal. They may also explain how T cells maintain sensitivity to antigens present in only low abundance on the antigen-presenting cell.
机译：T细胞通过其T细胞抗原受体（TCR）与与主要组织相容性复合物（MHC）分子结合的抗原肽的相互作用来启动许多免疫反应。这种相互作用通过一种尚不清楚的机制将生化信号发送到T细胞中。我们已经使用准弹性光散射（QELS）表明，在结合有完整激动剂肽的MHC分子存在的情况下，TCR /肽-MHC复合物在溶液中低聚形成超分子结构，其浓度接近于结合反应的解离常数。低聚物的大小与浓度有关，对于此处测试的浓度，计算得出其含有2至6个三元复合物。这种作用是特异的，因为除非正确的肽与MHC结合，否则分子本身不会形成寡聚物，也不会观察到寡聚物。这些结果为基于多个TCR /肽-MHC复合物的特定组装的T细胞信号传导模型提供了直接的证据，其中组装的程度决定了所转导信号的程度和定性。他们还可以解释T细胞如何保持对抗原呈递细胞仅以低丰度存在的抗原的敏感性。

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