The quail and chicken intestine have sialyl-galactose sugar chains responsible for the binding of influenza A viruses to human type receptors
The quail and chicken intestine have sialyl-galactose sugar chains responsible for the binding of influenza A viruses to human type receptors
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DOI：
10.1093/glycob/cwm038
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发表时间：
2007-07-01
期刊：
影响因子：
4.3
通讯作者：
Suzuki, Yasuo
中科院分区：
文献类型：
--
作者：
Guo, Chao-Tan;Takahashi, Noriko;Suzuki, Yasuo
流感病毒的受体特异性是允许禽流感病毒跨越物种屏障的因素之一。最近H5N1和H9N2型禽流感病毒从鸡和/或鹌鹑传播给人类的情况表明，禽类进入了。流感病毒可以直接感染人类，而不需要中间宿主，如猪。在这项研究中，我们使用了两株甲型流感病毒(A/PR/8/34，优先与禽型受体结合，以及A/孟菲斯/1/71，优先与人型受体结合)来探测宿主细胞中的受体特异性。禽类和鸡类肠道(结肠)上皮细胞均可与禽类和人型病毒结合。受感染的培养的鹌鹑结肠细胞表达病毒蛋白，并允许复制A/PR/8/34或A/孟菲斯/1/71病毒株。为了了解这些现象的分子基础，我们进一步研究了宿主细胞中通过α2-3连接(Siaα2-3Gal)和Siaa2-6Gal连接到半乳糖(Gal)上的唾液酸(Sia)的丰度。在鹌鹑和鸡结肠上皮细胞的糖蛋白和糖脂组分中，均含有Sia-Gal连锁特异性凝集素的结合组分：Maackia amurensis凝集素(专用于Siaα2-3 Gal)和接骨木凝集素(专用于Siaα2-6Gal)，表明Siaα2-3Gal和Siaα2-6Gal均存在于鹌鹑和鸡的结肠细胞中。此外，我们通过以下方式进行了演示。高效液相色谱分析表明5-N-乙酰神经氨酸是SIA的主要分子物种，并通过多维高效液相色谱图谱和基质辅助激光解吸/电离飞行时间质谱分析证明，鸡和鹌鹑肠道上皮组织表达的主要(79%以上)唾液酸半乳糖残基末端的双触角复合型糖链α2-6(S)。综上所述，这些结果表明，鹌鹑和鸡具有潜在的禽类中间宿主的分子特征。流感病毒会传播给人类，并可能产生具有大流行潜力的新流感病毒。
The receptor specificity of influenza viruses is one factor that allows avian influenza viruses to cross the species barrier. The recent transmissions of avian H5N1 and H9N2 influenza viruses from chickens and/ or quails to humans indicate that avian in. uenza viruses can directly infect humans without an intermediate host, such as pigs. In this study, we used two strains of influenza A virus (A/PR/8/34, which preferentially binds to an avian-type receptor, and A/Memphis/1/71, which preferentially binds to a human-type receptor) to probe the receptor specificities in host cells. Epithelial cells of both quail and chicken intestines (colons) could bind both avian-and human-type viruses. Infected cultured quail colon cells expressed viral protein and allowed replication of the virus strain A/PR/8/34 or A/Memphis/1/71. To understand the molecular basis of these phenomena, we further investigated the abundance of sialic acid (Sia) linked to galactose (Gal) by the alpha 2-3 linkage (Sia alpha 2-3Gal) and Siaa2-6Gal in host cells. In glycoprotein and glycolipid fractions from quail and chicken colon epithelial cells, there were some bound components of Sia-Gal linkage-specific lectins, Maackia amurensis agglutinin (specific for Sia alpha 2-3 Gal) and Sambucus nigra agglutinin (specific for Siaa2-6Gal), indicating that both Sia alpha 2-3Gal and Sia alpha 2-6Gal exist in quail and chicken colon cells. Furthermore, we demonstrated by. uorescence high-performance liquid chromatography (HPLC) analysis that 5-N-acetylneuraminic acid was the main molecular species of Sia, and we demonstrated by multi-dimensional HPLC mapping and matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry analysis that bi-antennary complex-type glycans alpha 2-6 sialylated at the terminal Gal residue(s) are major (more than 79%) sialyl N-glycans expressed by intestinal epithelial tissues in both the chicken and quail. Taken together, these results indicate that quails and chickens have molecular characterization as potential intermediate hosts for avian in. fluenza virus transmission to humans and could generate new influenza viruses with pandemic potential.