在FBL-3肿瘤细胞上表达的病毒编码辅助性T细胞表位的精细结构。
Fine structure of a virus-encoded helper T-cell epitope expressed on FBL-3 tumor cells.
作者信息
Shimizu T, Uenishi H, Teramura Y, Iwashiro M, Kuribayashi K, Tamamura H, Fujii N, Yamagishi H
机构信息
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
出版信息
J Virol. 1994 Dec;68(12):7704-8. doi: 10.1128/JVI.68.12.7704-7708.1994.
Abstract
Antigen peptide fn20 representing Friend murine leukemia virus env122-141 (DEPLTSLTPRCNTAWNRLKL) is recognized by two independent Friend virus-induced, FBL-3 tumor-specific helper T-cell (Th) clones. We isolated more Th clones from mice immunized with fn20 peptide. We examined the fine structure of the peptide required to activate a large group of fn20-specific Th clones. A systematic analysis of peptides of decreasing lengths eliciting Th proliferation defined the minimum core length as 13 amino acids (LTSLTPRCNTAWN). Functional proliferation and competition assays with variant peptides with alanine substitutions permitted the assignment of five peptide residues in two major histocompatibility complex-interacting and three T-cell-receptor-interacting sites. Th clones were different in their reactivities toward peptides of various lengths and the variant peptides.
摘要
代表弗氏小鼠白血病病毒env122 - 141（DEPLTSLTPRCNTAWNRLKL）的抗原肽fn20可被两个独立的、由弗氏病毒诱导的FBL - 3肿瘤特异性辅助性T细胞（Th）克隆识别。我们从用fn20肽免疫的小鼠中分离出了更多的Th克隆。我们研究了激活大量fn20特异性Th克隆所需的肽的精细结构。对引发Th增殖的长度递减的肽进行系统分析，确定最小核心长度为13个氨基酸（LTSLTPRCNTAWN）。用丙氨酸替代的变异肽进行功能增殖和竞争试验，确定了两个主要组织相容性复合体相互作用位点和三个T细胞受体相互作用位点中的五个肽残基。Th克隆对不同长度的肽和变异肽的反应性有所不同。
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