Crowley M P, Reich Z, Mavaddat N, Altman J D, Chien Y
Program in Immunology, Stanford University School of Medicine, California 94305, USA.
J Exp Med. 1997 Apr 7;185(7):1223-30. doi: 10.1084/jem.185.7.1223.
Recent studies have shown that many nonclassical major histocompatibility complex (MHC) (class 1b) molecules have distinct antigen-binding capabilities, including the binding of nonpeptide moieties and the binding of peptides that are different from those bound to classical MHC molecules. Here, we show that one of the H-2T region-encoded molecules, T10, when produced in Escherichia coli, can be folded in vitro with beta2-microglobulin (beta2m) to form a stable heterodimer in the absence of peptide or nonpeptide moieties. This heterodimer can be recognized by specific antibodies and is stimulatory to the gammadelta T cell clone, G8. Circular dichroism analysis indicates that T10/beta2m has structural features distinct from those of classical MHC class I molecules. These results suggest a new way for MHC-like molecules to adopt a peptide-free structure and to function in the immune system.
最近的研究表明，许多非经典主要组织相容性复合体（MHC）（1b类）分子具有独特的抗原结合能力，包括非肽部分的结合以及与经典MHC分子所结合的肽不同的肽的结合。在此，我们表明，H-2T区域编码的分子之一T10在大肠杆菌中产生时，可在体外与β2-微球蛋白（β2m）折叠，在不存在肽或非肽部分的情况下形成稳定的异二聚体。这种异二聚体可被特异性抗体识别，并对γδT细胞克隆G8具有刺激作用。圆二色性分析表明，T10/β2m具有与经典MHC I类分子不同的结构特征。这些结果提示了一种MHC样分子形成无肽结构并在免疫系统中发挥作用的新方式。
