Maksiutov A Z
Vopr Virusol. 1989 May-Jun;34(3):283-8.
The effect of amino acid substitutions within the antigenic sites, the residues close to these sites, and the other parts of the hemagglutinin molecule on cross-reactions between influenza subtype H3N2 virus strains in hemagglutination-inhibition tests are considered. Previously we reported a method for calculation of the values of immunochemical cross-reactions between the homologous proteins based on the structural data. On this basis, a method for calculation of the titers of cross-reactions of influenza viruses in hemagglutination-inhibition tests is proposed. The values obtained by this method show a good correlation with the known experimental data. Analysis of the nature of amino acid replacements in region D located in the interface between the hemagglutinin subunits has shown that this region cannot bind with antibodies. The data on the limitation of the resource of the subtype H3N2 variability are presented.
研究了抗原位点内的氨基酸取代、靠近这些位点的残基以及血凝素分子其他部分对血凝抑制试验中H3N2流感病毒株之间交叉反应的影响。此前我们报道了一种基于结构数据计算同源蛋白间免疫化学交叉反应值的方法。在此基础上，提出了一种计算血凝抑制试验中流感病毒交叉反应滴度的方法。用该方法获得的值与已知实验数据具有良好的相关性。对位于血凝素亚基之间界面的D区氨基酸替换性质的分析表明，该区域不能与抗体结合。给出了H3N2亚型变异性资源有限的数据。
