HLA I类分子与肽广泛结合的证据。
Evidence of widespread binding of HLA class I molecules to peptides.
作者信息
Frelinger J A, Gotch F M, Zweerink H, Wain E, McMichael A J
机构信息
Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, United Kingdom.
出版信息
J Exp Med. 1990 Sep 1;172(3):827-34. doi: 10.1084/jem.172.3.827.
Abstract
We have tested the binding of HLA class I proteins to peptides using a solid-phase binding assay. We tested 102 peptides, mostly derived from the HIV gag and HIV pol sequences. Most peptides did not bind to any class I protein tested. The pattern of binding among the three class I proteins tested, HLA-A2, -B27, and -B8, was approximately 85% concordant. Further, all five of the known HIV-1 gag T cell epitopes detected by human CTL bound at least one class I protein. Binding of class I to the peptides could be detected either by directly iodinated class I proteins, or indirectly using monoclonal antibodies specific for class I. The binding to the plates could be blocked with MA2.1, which binds in the alpha 1 region of A2, but not by W6/32, which binds elsewhere. The data presented here show that binding of class I to peptides is specific, but that many peptides bind to more than a single class I protein.
摘要
我们使用固相结合试验检测了HLA I类蛋白与肽段的结合情况。我们测试了102个肽段，大多源自HIV gag和HIV pol序列。大多数肽段不与所检测的任何I类蛋白结合。所检测的三种I类蛋白HLA - A2、- B27和- B8之间的结合模式约85%一致。此外，人CTL检测到的所有五个已知HIV - 1 gag T细胞表位至少与一种I类蛋白结合。I类蛋白与肽段的结合既可以通过直接碘化的I类蛋白检测，也可以使用针对I类蛋白的单克隆抗体间接检测。与平板的结合可以被MA2.1阻断，MA2.1在A2的α1区域结合，但不能被在其他位置结合的W6/32阻断。此处呈现的数据表明I类蛋白与肽段的结合具有特异性，但许多肽段能与不止一种I类蛋白结合。
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