Mateu M G, Andreu D, Carreño C, Roig X, Cairó J J, Camarero J A, Giralt E, Domingo E
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, Spain.
Eur J Immunol. 1992 Jun;22(6):1385-9. doi: 10.1002/eji.1830220609.
Synthetic peptides have been used to mimic the main antigenic site of foot-and-mouth disease virus (FMDV) of serotype C and of several variant isolates. This region includes multiple continuous B cell epitopes. The effect of single amino acid replacements, individually or in combination, on antigen specificity has been evaluated using monoclonal antibodies. Quantitative enzyme immunodot assays have shown that both additive and non-additive effects of multiple replacements occur in continuous B cell epitopes, with regard to antibody recognition. Antigenically critical single replacements may be compensated by other, non-critical replacements. Thus, the role of a single amino acid on antibody recognition depends on the sequence context in the antigenic domain. The non-additive effects of multiple replacements may modulate the extent of antigenic diversification of highly variable RNA viruses, and keep viruses confined within antigenic groups by precluding linear antigenic divergence.
合成肽已被用于模拟C型口蹄疫病毒（FMDV）及几种变异分离株的主要抗原位点。该区域包含多个连续的B细胞表位。已使用单克隆抗体评估了单个氨基酸替换单独或组合对抗原特异性的影响。定量酶免疫斑点试验表明，就抗体识别而言，多个替换在连续B细胞表位中会产生累加和非累加效应。抗原性关键的单个替换可能会被其他非关键替换所补偿。因此，单个氨基酸对抗体识别的作用取决于抗原结构域中的序列背景。多个替换的非累加效应可能会调节高变RNA病毒的抗原多样化程度，并通过防止线性抗原差异将病毒限制在抗原组内。
