Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species
Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species
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DOI：
10.1006/viro.1996.8323
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发表时间：
1997-01-20
期刊：
影响因子：
3.7
通讯作者：
Kawaoka, Y
中科院分区：
文献类型：
--
作者：
Ito, T;Suzuki, Y;Kawaoka, Y
尽管甲型流感病毒与含寡糖末端唾液酸的结合能力一致，但其受体特异性却存在差异。为了测试来自不同动物物种的红细胞的凝集是否可用于评估甲型流感病毒的受体特异性，我们使用来自七种动物物种的红细胞确定了一系列病毒株的凝集活性，包括具有已知受体特异性的病毒株的凝集活性。所有马和禽病毒，包括已知识别通过 α 2,3 连接与半乳糖连接的 N-乙酰基和 N-羟乙酸唾液酸的病毒（NeuAc α 2,3Gal 和 NeuGc α 2,3Gal），都会凝集来自所有测试动物物种（鸡、鸭、豚鼠、人类、绵羊、马和牛）的红细胞。人类病毒，包括已知优先识别 NeuAc α 2,6Gal 的病毒，凝集了除马和牛红细胞之外的所有红细胞。使用连锁特异性凝集素 [黑接骨木凝集素用于唾液酸 (SA)α 2,6Gal 和 Maackia amurensis 凝集素用于 SA α 2,3Gal] 对红细胞进行荧光激活细胞分选分析表明，牛和马红细胞均含有大量 SA α 2,3Gal，但几乎没有 SA2,6Gal 特异性凝集素反应细胞表面含有寡糖，而人类和鸡的红细胞都含有这两种类型的寡糖。考虑到马和牛红细胞中的大多数（>93%）唾液酸是 N-乙醇酰类型，我们的结果表明能够凝集这些红细胞的病毒（即禽和马病毒）识别 NeuGc α 2,3Gal。这些发现还表明，使用来自不同动物物种的红细胞进行凝集测定将有助于表征甲型流感病毒的受体特异性。 (C) 1997 学术出版社
Despite their uniform ability to bind to oligosaccharide-containing terminal sialic acids, influenza A viruses show differences in receptor specificity. To test whether agglutination of erythrocytes from different animal species could be used to assess the receptor specificity of influenza A viruses, we determined the agglutinating activities of a range of virus strains, including those with known receptor specificities, using erythrocytes from seven animal species. All equine and avian viruses, including those known to recognize N-acetyl and N-glycolyl sialic acid linked to galactose by the alpha 2,3 linkage (NeuAc alpha 2,3Gal and NeuGc alpha 2,3Gal), agglutinated erythrocytes from all of the animal species tested (chickens, ducks, guinea pigs, humans, sheep, horses, and cows). The human viruses, including those known to preferentially recognize NeuAc alpha 2,6Gal, agglutinated all but the horse and cow erythrocytes. Fluorescence-activated cell sorting analysis of erythrocytes using linkage-specific lectins [Sambucus nigra agglutinin for sialic acid (SA)alpha 2,6Gal and Maackia amurensis agglutinin for SA alpha 2,3Gal] showed that both cow and horse erythrocytes contain a large amount of SA alpha 2,3Gal-, but virtually no SA2,6Gal-specific lectin-reactive oligosaccharides on the cell surface, while human and chicken erythrocytes contained both types of oligosaccharides. Considering that the majority (>93%) of sialic acid in horse and cow erythrocytes is of the N-glycolyl type, our results suggest that viruses able to agglutinate these erythrocytes (i.e., avian and equine viruses) recognize NeuGc alpha 2,3Gal. These findings also show that agglutinating assays with erythrocytes from different animal species would be useful in characterizing the receptor specificity of influenza A viruses. (C) 1997 Academic Press