van Binnendijk R S, Versteeg-van Oosten J P, Poelen M C, Brugghe H F, Hoogerhout P, Osterhaus A D, Uytdehaag F G
Laboratory of Immunobiology, National Institute of Public Health and Environmental Protection, Bilthoven, The Netherlands.
J Virol. 1993 Apr;67(4):2276-84. doi: 10.1128/JVI.67.4.2276-2284.1993.
The transmembrane fusion (F) glycoprotein of measles virus is an important target antigen of human HLA class I- and class II-restricted cytotoxic T lymphocytes (CTL). Genetically engineered F proteins and nested sets of synthetic peptides spanning the F protein were used to determine sequences of F recognized by a number of F-specific CTL clones. Combined N- and C-terminal deletions of the respective peptides revealed that human HLA class I and HLA class II-restricted CTL efficiently recognize nonapeptides or decapeptides representing epitopes of F. Three distinct sequences recognized by three different HLA class II (DQw1, DR2, and DR4/w53)-restricted CTL clones appear to cluster between amino acids 379 and 466 of F, thus defining an important T-cell epitope area of F. Within this same region, a nonamer peptide of F was found to be recognized by an HLA-B27-restricted CTL clone, as expected on the basis of the structural homology between this peptide and other known HLA-B27 binding peptides.
麻疹病毒的跨膜融合(F)糖蛋白是人类HLA I类和II类限制性细胞毒性T淋巴细胞(CTL)的重要靶抗原。利用基因工程改造的F蛋白和跨越F蛋白的一系列嵌套合成肽,确定了多个F特异性CTL克隆识别的F序列。对相应肽段进行N端和C端联合缺失分析表明,人类HLA I类和II类限制性CTL能有效识别代表F表位的九肽或十肽。三个不同的HLA II类(DQw1、DR2和DR4/w53)限制性CTL克隆识别的三个不同序列似乎聚集在F蛋白的379至466位氨基酸之间,从而确定了F的一个重要T细胞表位区域。在同一区域内,发现F的一个九肽能被一个HLA - B27限制性CTL克隆识别,基于该肽与其他已知HLA - B27结合肽之间的结构同源性,这是预期的结果。