Matsuzaki M, Sugawara K, Adachi K, Hongo S, Nishimura H, Kitame F, Nakamura K
Department of Bacteriology, Yamagata University School of Medicine, Japan.
Virology. 1992 Jul;189(1):79-87. doi: 10.1016/0042-6822(92)90683-g.
Neutralization-resistant variants of influenza C/Ann Arbor/1/50 virus were selected with monoclonal antibodies against four different antigenic sites on the hemagglutinin-esterase (HE) glycoprotein, and their HE genes were sequenced to identify amino acid residues important for the integrity of each site. Twelve different amino acid substitutions in a total of 18 antigenic variants were all located on the HE1 subunit. Although variants for antigenic site A-2 had a change at position 367, all substitutions in the variants for sites A-1, A-3, and A-4 occurred in the central region of the HE1 spanning amino acid positions 178 to 283. Furthermore, it was found that many of the substitutions in the variants selected with antibodies to sites A-1 and A-3 were clustered within or near one of the three variable regions revealed previously by comparing amino acid sequences of the HEs among various influenza C isolates (Buonagurio, D. A., Nakada, S., Fitch, W. M., and Palese, P., Virology 146, 221-232, 1985). The antigenic variants were also examined for their ability to agglutinate chicken and human erythrocytes in order to obtain information concerning the receptor-binding site on the HE molecule. The results suggested that the amino acid changes at residues 178, 186, 187, 190, 206, 212, and 226 decreased the hemagglutinating activity whereas those at residues 245, 266, and 283 produced an opposite effect.
用针对血凝素酯酶（HE）糖蛋白上四个不同抗原位点的单克隆抗体筛选出了抗甲型流感病毒/安阿伯/1/50病毒的中和抗性变体，并对其HE基因进行测序，以确定对每个位点完整性至关重要的氨基酸残基。在总共18个抗原变体中的12个不同氨基酸取代均位于HE1亚基上。虽然抗原位点A-2的变体在第367位发生了变化，但位点A-1、A-3和A-4的变体中的所有取代都发生在HE1的中央区域，该区域跨越氨基酸位置178至283。此外，还发现用针对位点A-1和A-3的抗体筛选出的变体中的许多取代聚集在先前通过比较各种甲型流感病毒分离株的HE氨基酸序列而揭示的三个可变区域之一内或附近（Buonagurio，D.A.，Nakada，S.，Fitch，W.M.和Palese，P.，《病毒学》146，221 - 232，1985）。还检测了抗原变体凝集鸡和人红细胞的能力，以获取有关HE分子上受体结合位点的信息。结果表明，第178、186、187、190、206、212和226位的氨基酸变化降低了血凝活性，而第245、266和283位的氨基酸变化则产生了相反的效果。
