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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Isolation of HLA-DR1·(staphylococcal enterotoxin A)_2 trimers in solution
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Isolation of HLA-DR1·(staphylococcal enterotoxin A)_2 trimers in solution

机译：溶液中HLA-DR1·（葡萄球菌肠毒素A）_2三聚体的分离

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摘要

Mutational studies indicate that the super-antigen staphylococcal enterotoxin A (SEA) has two separate binding sites for major histocompatibility complex (MHC) class Ⅱ molecules. Direct evidence is provided here for the formation of SEA-MHC class Ⅱ trimers in solution. Isoelec-tric focusing separated SEA-HLA-DR1 complexes into both dimers and HLA-DR1·SEA_2 trimers. The molar ratio of components was determined by dual isotope labeling. The SEA mutant SEA-F47S, L48S, Y92A, which is deficient in MHC class Ⅱ α-chain binding, formed only dimers with HLA-DR1, whereas a second SEA mutant, SEA-H225A, which lacks high-affinity MHC class Ⅱ β-chain binding was incapable of forming any complexes. Thus SEA binding to its MHC receptor is a two-step process involving initial β-chain binding followed by cooperative binding of a second SEA molecule to the class Ⅱ α chain.
机译：突变研究表明，超抗原葡萄球菌肠毒素A（SEA）具有两个独立的主要组织相容性复合体（MHC）Ⅱ类分子结合位点。这里提供了在溶液中形成SEA-MHCⅡ类三聚体的直接证据。等电聚焦将SEA-HLA-DR1复合物分为二聚体和HLA-DR1·SEA_2三聚体。组分的摩尔比通过双重同位素标记确定。缺乏MHCⅡ类α链结合的SEA突变SEA-F47S，L48S，Y92A仅与HLA-DR1形成二聚体，而第二个SEA突变SEA-H225A缺乏MHCⅡ类高亲和力-链结合不能形成任何复合物。因此，SEA与其MHC受体的结合是一个两步过程，涉及初始的β链结合，然后将第二个SEA分子协同结合到Ⅱ类α链。

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