Drescher J, Verhagen W
Institute of Virology, Medical School of Hannover, Germany.
J Virol Methods. 1993 Apr;42(1):75-88. doi: 10.1016/0166-0934(93)90178-t.
A method described previously for determining the concentration of influenza virus antihemagglutinin antibody molecules, the number of epitopes per virus particle and the equilibrium constant of virus antibody interaction was adapted to the use with escape variants (EVs), produced by multiplication of influenza virus A/Brazil (H1N1) in presence of monoclonal antibody directed to each of the four hemagglutinin sites (Sa, Sb, Ca and Cb). The EVs were found to possess an altered antigenic site, which was both antigenic and immunogenic. By use of selected EVs and antibody preparations, the number of epitopes per antigenic site was determined and it was found that each of the four sites was represented by about 390 epitopes per virus particle, suggesting that each of the about 400 hemagglutinin spikes per virion possessed one epitope of the specificity Sa, Sb, Ca and Cb. Alteration of site Sa but not of site Ca increased the avidity of antibody to react with the unchanged sites.
先前描述的一种用于测定流感病毒抗血凝素抗体分子浓度、每个病毒颗粒的表位数量以及病毒-抗体相互作用平衡常数的方法，被应用于由甲型/巴西（H1N1）流感病毒在针对四个血凝素位点（Sa、Sb、Ca和Cb）中每一个的单克隆抗体存在下增殖所产生的逃逸变异株（EVs）。发现这些逃逸变异株具有一个改变的抗原位点，该位点兼具抗原性和免疫原性。通过使用选定的逃逸变异株和抗体制剂，确定了每个抗原位点的表位数量，并且发现四个位点中的每一个在每个病毒颗粒中大约由390个表位代表，这表明每个病毒粒子中约400个血凝素刺突中的每一个都具有特异性为Sa、Sb、Ca和Cb的一个表位。位点Sa而非位点Ca的改变增加了抗体与未改变位点反应的亲和力。
