Ferrier P, Fontecilla-Camps J C, Bucchini D, Caillol D H, Jordan B R, Lemonnier F A
Immunogenetics. 1985;21(4):321-31. doi: 10.1007/BF00430798.
The serological reactivities of HLA-A3, -B7, and -CW3 heavy chains associated with either mouse, bovine, or human beta-2-microglobulin (beta 2m) and expressed on the surface of transfected mouse fibroblasts were analyzed. All reactivities associated with one cluster (defined by monoclonal antibody W6/32) of antigenic determinants expressed by these HLA class I molecules were lost, or profoundly reduced, after each heavy chain associated with mouse beta 2-m. Expression by the transfected fibroblasts of the HLA-A3, -B7, and -CW3 heavy chains in association with human beta 2m restores these reactivities. Since most of the amino acid differences between mouse and human beta 2m probably correspond to externally oriented hydrophilic residues, these results suggest that critical interactions in the three-dimensional structure of HLA class I molecules occur between the light chain and the first two external domains of the class I heavy chains, to which some of the altered reactivities have been mapped.
分析了与小鼠、牛或人β2-微球蛋白（β2m）相关并在转染的小鼠成纤维细胞表面表达的HLA-A3、-B7和-CW3重链的血清学反应性。在每条与小鼠β2m相关的重链后，与这些HLA I类分子表达的一个抗原决定簇簇（由单克隆抗体W6/32定义）相关的所有反应性均丧失或显著降低。转染的成纤维细胞中HLA-A3、-B7和-CW3重链与人类β2m的结合恢复了这些反应性。由于小鼠和人类β2m之间的大多数氨基酸差异可能对应于外部取向的亲水性残基，这些结果表明，HLA I类分子三维结构中的关键相互作用发生在轻链和I类重链的前两个外部结构域之间，一些改变的反应性已被定位到这些结构域。
