Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity.
Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity.
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发表时间：
1990
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通讯作者：
L. Baum;J. Paulson
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作者：
L. Baum;J. Paulson
甲型流感病毒的人H3毒株优先结合含有序列NeuAc α 2，6 Gal的细胞表面寡糖，而禽流感毒株优先识别序列NeuAc α 2，3Gal。这两种类型的唾液酸键在宿主呼吸道上皮细胞（流感感染的靶细胞）上的分布可能是选择在人和禽流感毒株中观察到的不同受体特异性的一个因素。为了研究这两种结构在人气管上皮细胞上的分布，使用了两种唾液酸特异性凝集素。黑接骨木凝集素（SNA）识别NeuAc α 2，6 Gal/GalNac序列，主要结合纤毛气管上皮细胞的表面，并且仅弱结合表面杯状细胞中的粘蛋白。相反，对NeuAc α 2，3Gal序列具有特异性的怀槐凝集素（MAL）强烈结合杯状细胞中的粘液滴，但不结合纤毛细胞的表面。因此，人纤毛气管细胞似乎含有优先被人流感病毒株识别的唾液酸寡糖。这些发现表明，人类H3流感病毒株可能已经进化出一种受体特异性，这种特异性有利于与纤毛细胞结合，并使呼吸道粘液的结合抑制最小化。
Human H3 strains of influenza A virus preferentially bind cell-surface oligosaccharides containing the sequence NeuAc alpha 2,6Gal, while avian influenza strains preferentially recognize the sequence NeuAc alpha 2,3Gal. The distribution of these two types of sialic acid linkages on host respiratory epithelium, the target of influenza infection, may be a factor in the selection of the different receptor specificities observed in human and avian influenza strains. To examine the distribution of these two structures on human tracheal epithelial cells, two sialic acid specific lectins were used. The Sambucus nigra lectin (SNA), which recognizes the sequence NeuAc alpha 2,6Gal/GalNac, primarily binds to the surface of the ciliated tracheal epithelial cells, and only weakly binds to mucins in the surface goblet cells. In contrast, the Maackia amurensis lectin (MAL), which is specific for the NeuAc alpha 2,3Gal sequence, binds strongly to mucus droplets in goblet cells, but not to the surface of ciliated cells. Thus, human ciliated tracheal cells appear to contain sialyloligosaccharides preferentially recognized by human influenza strains. These findings suggest that human H3 influenza strains may have evolved a receptor specificity which favors binding to ciliated cells, and minimizes binding inhibition by respiratory mucus.