Herman A, Croteau G, Sekaly R P, Kappler J, Marrack P
Howard Hughes Medical Institute, Department of Medicine, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado 80206.
J Exp Med. 1990 Sep 1;172(3):709-17. doi: 10.1084/jem.172.3.709.
Staphylococcal enterotoxins (SEs) have been shown to bind to major histocompatibility complex (MHC) class II proteins and stimulate T cells in a V beta-specific manner, and these V beta specificities for various SEs have been well documented in mice and humans. This study was undertaken in order to examine the ability of human class II molecules to present SEs to human and murine T cell hybridomas. Using a panel of transfectants expressing individual HLA class II antigens, we have shown that HLA-DR alleles differ in their ability to bind and present SEs. Since the HLA-DR proteins share a common alpha chain, these results indicate that the polymorphic beta chain plays an important role in SE binding and presentation to T cells. In addition, we have shown that human class II isotypes markedly differ in their ability to present SEs. The results of this study should provide information on the region of MHC class II molecules that interacts with foreign, and perhaps self, super-antigens.
葡萄球菌肠毒素(SEs)已被证明可与主要组织相容性复合体(MHC)II类蛋白结合,并以Vβ特异性方式刺激T细胞,而且这些不同SEs的Vβ特异性在小鼠和人类中已有充分记载。进行这项研究是为了检测人类II类分子将SEs呈递给人类和鼠类T细胞杂交瘤的能力。使用一组表达单个HLA II类抗原的转染细胞,我们发现HLA-DR等位基因在结合和呈递SEs的能力上存在差异。由于HLA-DR蛋白共享一条共同的α链,这些结果表明多态性的β链在SE与T细胞的结合及呈递过程中起重要作用。此外,我们还表明人类II类同种型在呈递SEs的能力上有显著差异。这项研究的结果应能提供有关MHC II类分子与外来超抗原,或许还有自身超抗原相互作用区域的信息。