Gairin J E, Oldstone M B
Laboratoire de Pharmacologie et Toxicologie Fondamentales, Centre National de la Recherche Scientifique, Toulouse, France.
J Virol. 1993 May;67(5):2903-7. doi: 10.1128/JVI.67.5.2903-2907.1993.
Viral antigens are presented to cytotoxic T lymphocytes (CTLs) by H-2-restricted major histocompatibility complex (MHC) glycoproteins. Binding of the endogenously processed viral peptides (epitopes) to their specific MHC molecules is an early intracellular event in the recognition process and is necessary for subsequent killing of virus-infected cells by virus-specific CTLs. It is now well established that interaction between a viral antigenic peptide and MHC is dependent on the primary structure (length and amino acid sequence) of that antigen. Here we show, using the H-2Db-restricted epitope GP277-286 of lymphocytic choriomeningitis virus as a model, that the secondary structure (conformation) of the viral sequence also plays a crucial role in the binding of a viral antigen to MHC glycoprotein and in its subsequent presentation to virus-specific CTLs.
病毒抗原通过H-2限制性主要组织相容性复合体(MHC)糖蛋白呈递给细胞毒性T淋巴细胞(CTL)。内源性加工的病毒肽(表位)与其特异性MHC分子的结合是识别过程中的早期细胞内事件,对于随后病毒特异性CTL杀伤病毒感染细胞是必要的。现已充分证实,病毒抗原肽与MHC之间的相互作用取决于该抗原的一级结构(长度和氨基酸序列)。在此,我们以淋巴细胞性脉络丛脑膜炎病毒的H-2Db限制性表位GP277-286为模型,表明病毒序列的二级结构(构象)在病毒抗原与MHC糖蛋白的结合及其随后呈递给病毒特异性CTL的过程中也起着关键作用。