IDENTIFICATION OF A CD4 BINDING-SITE ON THE BETA-2-DOMAIN OF HLA-DR MOLECULES
IDENTIFICATION OF A CD4 BINDING-SITE ON THE BETA-2-DOMAIN OF HLA-DR MOLECULES
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DOI：
10.1038/356799a0
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发表时间：
1992-04-30
期刊：
影响因子：
64.8
通讯作者：
SINIGAGLIA, F
中科院分区：
文献类型：
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作者：
CAMMAROTA, G;SCHEIRLE, A;SINIGAGLIA, F
CD 4和CD 8分子是由功能不同的成熟T细胞亚群表达的跨膜糖蛋白。CD 4+和CD 8 + T细胞分别识别携带主要组织相容性复合体（MHC）II类和携带I类的靶细胞上的抗原1-3。抗CD 4和CD 8的单克隆抗体阻断T细胞识别抗原的能力，以及细胞-细胞粘附试验4-7表明，CD 4和CD 8与II类或I类MHC的非多态性决定簇结合。在这里，我们证明了可溶性重组HLA-DR 4分子从昆虫细胞和HLA-DR衍生肽结合到固定的重组可溶性CD 4。CD 4结合重组可溶性DR 4异二聚体，以及单独的可溶性DR 4-β链。此外，12个DR 4-β-肽中的两个可以与CD 4特异性相互作用。这些发现表明，CD 4与MHC II类分子的一个区域相互作用，该区域类似于先前在结合CD 8的I类MHC蛋白中鉴定的环（参考文献8、9）。
THE CD4 and CD8 molecules are transmembrane glycoproteins expressed by functionally distinct subsets of mature T cells. CD4+ and CD8+ T cells recognize antigens on major histocompatibility complex (MHC) class II-bearing and class I-bearing target cells respectively 1-3. The ability of monoclonal antibodies against CD4 and CD8 to block antigen recognition by T cells, as well as cell-cell adhesion assays 4-7, indicate that CD4 and CD8 bind to non-polymorphic determinants of class II or class I MHC. Here we demonstrate that soluble recombinant HLA-DR4 molecules from insect cells and HLA-DR-derived peptides bind to immobilized recombinant soluble CD4. CD4 binds recombinant soluble DR4 heterodimers, as well as the soluble DR4-beta-chain alone. Furthermore, two out of twelve DR4-beta-peptides could interact specifically with CD4. These findings show that CD4 interacts with a region of MHC class II molecules analogous to a previously identified loop in class I MHC proteins that binds CD8 (refs 8,9).