Ito T, Suzuki Y, Mitnaul L, Vines A, Kida H, Kawaoka Y
Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Virology. 1997 Jan 20;227(2):493-9. doi: 10.1006/viro.1996.8323.
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 alpha2,3 linkage (NeuAc alpha2,3Gal and NeuGc alpha2,3Gal), 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 alpha2,6Gal, 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) alpha2,6Gal and Maackia amurensis agglutinin for SA alpha2,3Gal] showed that both cow and horse erythrocytes contain a large amount of SA alpha2,3Gal-, 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 alpha2,3Gal. 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.
尽管甲型流感病毒都具有结合含寡糖末端唾液酸的能力，但它们在受体特异性上存在差异。为了测试来自不同动物物种的红细胞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，测定了一系列病毒株（包括那些具有已知受体特异性的病毒株）的凝集活性。所有马源和禽源病毒，包括那些已知能识别通过α2,3键与半乳糖相连的N-乙酰和N-糖基化唾液酸（NeuAcα2,3Gal和NeuGcα2,3Gal）的病毒，都能凝集所有测试动物物种（鸡、鸭、豚鼠、人、绵羊、马和牛）的红细胞。人源病毒，包括那些已知优先识别NeuAcα2,6Gal的病毒，能凝集除马和牛红细胞外的所有红细胞。使用连接特异性凝集素（用于唾液酸（SA）α2,6Gal的黑接骨木凝集素和用于SAα2,3Gal的山嵛菜凝集素）对红细胞进行荧光激活细胞分选分析表明，牛和马的红细胞都含有大量的SAα2,3Gal -，但细胞表面几乎没有SA2,6Gal特异性凝集素反应性寡糖，而人和鸡的红细胞则含有这两种类型的寡糖。考虑到马和牛红细胞中大多数（>93%）的唾液酸是N-糖基化类型，我们的结果表明，能够凝集这些红细胞的病毒（即禽源和马源病毒）识别NeuGcα2,3Gal。这些发现还表明，用来自不同动物物种的红细胞进行凝集试验，将有助于表征甲型流感病毒的受体特异性。
