Ou D, Chong P, Choi Y, McVeigh P, Jefferies W A, Koloitis G, Tingle A J, Gillam S
Department of Pathology, University of British Columbia, Vancouver, Canada.
J Virol. 1992 Nov;66(11):6788-93. doi: 10.1128/JVI.66.11.6788-6793.1992.
T-cell epitopes on the E2 protein of rubella virus were studied by using 15 overlapping synthetic peptides covering the E2 protein sequence. The most frequently recognized epitopes on E2 were E2-4 (residues 54 to 74), with 5 of 10 tested T-cell lines responding to it. Two CD4+ cytotoxic T-cell cloned isolated from one T-cell line responded strongly in proliferation assays with peptide E2-4 and were cytotoxic to target cells presenting the E2-4 determinant. Truncated peptides contained within the E2-4 peptide sequence were used to define the T-cell determinants. Results indicated that amino acid residues 54 to 65 were directly involved. Human cell lines with different HLA phenotypes were tested for the capacity to present the antigenic determinants. The results suggested that recognition of peptide E2-4 by T-cell clones was associated with HLA DR7.
通过使用覆盖风疹病毒E2蛋白序列的15个重叠合成肽，对风疹病毒E2蛋白上的T细胞表位进行了研究。E2上最常被识别的表位是E2-4（第54至74位氨基酸残基），在10个测试的T细胞系中有5个对其产生反应。从一个T细胞系中分离出的两个CD4 + 细胞毒性T细胞克隆，在与肽E2-4进行的增殖试验中反应强烈，并且对呈递E2-4决定簇的靶细胞具有细胞毒性。E2-4肽序列中包含的截短肽被用于确定T细胞决定簇。结果表明，第54至65位氨基酸残基直接参与其中。对具有不同HLA表型的人细胞系呈递抗原决定簇的能力进行了测试。结果表明，T细胞克隆对肽E2-4的识别与HLA DR7相关。
