ISOLATION AND CHARACTERIZATION OF ANTIGEN-IA COMPLEXES INVOLVED IN T-CELL RECOGNITION
ISOLATION AND CHARACTERIZATION OF ANTIGEN-IA COMPLEXES INVOLVED IN T-CELL RECOGNITION
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DOI：
10.1016/0092-8674(86)90822-6
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发表时间：
1986-12-26
期刊：
影响因子：
64.5
通讯作者：
GREY, HM
中科院分区：
文献类型：
--
作者：
BUUS, S;SETTE, A;GREY, HM
使用平衡透析，先前已经证明免疫原性肽特异性结合Ia分子，Ia分子在对这些抗原的免疫应答中充当限制性元件。使用凝胶过滤来研究卵清蛋白（OVA）肽-I-Ad复合物的形成，在此证明，一旦形成复合物，该复合物是非常稳定的（kd约等于3倍。10-6 s-1），但复合物形成的速率非常慢（ka = 1）。1 M-1 s-1），解释了总的低平衡常数apx。2倍。10-6 M.用戊二醛处理复合物显示卵清蛋白肽仅与α-氨基端交联。I-Ad链含有I-Ad-OVA复合物的平面膜刺激T细胞应答，用2 ×比使用未复合抗原时所需的抗原少104，从而证明了这些复合物在抗原识别中的生物学重要性。
Using equilibrium dialysis, it has been previously demonstrated that immunogenic peptides bind specifically to the Ia molecules serving as restriction elements in the immune response to these antigens. Using gel filtration to study the formation of ovalbumin (OVA) peptide-I-Ad complexes, it is herein demonstrated that the complexes, once formed, are very stable (kd .apprxeq. 3 .times. 10-6 s-1), but the rate of complex formation is very slow (ka .apprxeq. 1 M-1 s-1), explaining the overall low equilibrium constant of .apprx. 2 .times. 10-6 M. Treating the complexes with glutaraldehyde revealed that the ovalbumin peptide was cross-linked solely to the .alpha. chain of I-Ad. Planar membranes containing I-Ad-OVA complexes stimulated a T cell response with 2 .times. 104 less antigen than required when uncomplexed antigen was used, thus demonstrating the biologic importance of these complexes in antigen recognition.