Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses
Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses
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DOI：
10.1007/s10719-008-9193-x
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发表时间：
2009-05-01
影响因子：
3
通讯作者：
Suzuki, Yasuo
中科院分区：
文献类型：
--
作者：
Sriwilaijaroen, Nongluk;Kondo, Sachiko;Suzuki, Yasuo
流感病毒感染的第一步是病毒血凝素与宿主细胞表面聚糖受体的特异性结合。甲型流感病毒对宿主的特异性是由病毒包膜血凝素介导的，血凝素与含有末端唾液酸聚糖的受体结合。人病毒优先结合宿主细胞受体上的α 2 -> - 6连接的唾液酸，而禽流感病毒特异性结合靶细胞上的α 2 -> - 3连接。人流感病毒分离物感染羊膜（AM）细胞比感染绒毛膜尿囊膜（CAM）细胞更有效。从10日龄鸡胚蛋的AM和CAM细胞中分离到n -聚糖，采用多维HPLC图谱和MALDI-TOF-MS技术分析了n -聚糖的结构。两种细胞的末端n -乙酰神经氨酸含量相似。在CAM细胞和AM细胞中，α 2 -> - 3连锁分子的摩尔百分比分别为27.2%和15.4%，而在人流感病毒中，α 2 -> - 6连锁分子的摩尔百分比分别为8.3 （CAM）和14.2% （AM）。人流感病毒识别的硫酸化聚糖在CAM和AM细胞中的摩尔百分比分别为3.8%和12.7%。这些结果揭示了CAM和AM细胞中n -聚糖的结构和摩尔百分比在决定人类和禽流感病毒感染和病毒适应方面的重要作用。
The initial step essential in influenza virus infection is specific binding of viral hemagglutinin to host cell-surface glycan receptors. Influenza A virus specificity for the host is mediated by viral envelope hemagglutinin, that binds to receptors containing glycans with terminal sialic acids. Human viruses preferentially bind to alpha 2 -> 6 linked sialic acids on receptors of host cells, whereas avian viruses are specific for the alpha 2 -> 3 linkage on the target cells. Human influenza virus isolates more efficiently infect amniotic membrane (AM) cells than chorioallantoic membrane (CAM) cells. N-glycans were isolated from AM and CAM cells of 10-day-old chicken embryonated eggs and their structures were analyzed by multi-dimensional HPLC mapping and MALDI-TOF-MS techniques. Terminal N-acetylneuraminic acid contents in the two cell types were similar. However, molar percents of alpha 2 -> 3 linkage preferentially bound by avian influenza virus were 27.2 in CAM cells and 15.4 in AM cells, whereas those of alpha 2 -> 6 linkage favored by human influenza virus were 8.3 (CAM) and 14.2 (AM). Molar percents of sulfated glycans, recognized by human influenza virus, in CAM and AM cells were 3.8 and 12.7, respectively. These results have revealed structures and molar percents of N-glycans in CAM and AM cells important in determining human and avian influenza virus infection and viral adaptation.