Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection
Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection
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DOI：
10.1042/bj3180389
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发表时间：
1996-09-01
影响因子：
4.1
通讯作者：
Suzuki, Y
中科院分区：
文献类型：
--
作者：
Suzuki, T;Sometani, A;Suzuki, Y
我们发现，通过使用病毒覆盖试验，甲型流感病毒分离株与硫苷脂（HSO 3-Gal β 1-> 1 'Cer）结合，硫苷脂没有唾液酸残基，并且人流感病毒A/孟菲斯/1/71（H3 N2）感染Madin-Darby犬肾细胞受到硫苷脂的抑制。A/孟菲斯/1/71（H3N2）引起用硫苷脂重构的无唾液酸红细胞的明显血凝和低pH溶血。到目前为止，所有来自试验动物种属的甲型流感病毒分离株均与硫苷脂结合。分离株的硫酸盐结合特异性不同于病毒唾液酸连接特异性。在病毒覆盖试验中，甲型流感病毒分离株也与半乳糖基神经酰胺（GalCer; Gal β 1-> 1'Cer）以及硫苷脂结合。相反。流感病毒不与N-脱酰基、硫苷脂的衍生物、葡糖基神经酰胺或其它测试的中性糖脂结合。这些结果表明半乳糖或硫酸化半乳糖与神经酰胺的连接对于病毒结合是重要的。
We found, by using a virus overlay assay, that influenza A virus isolates bind to sulphatide (HSO3-Gal beta 1 --> 1'Cer), which has no sialic acid residue, and that the infection of Madin-Darby canine kidney cells with the human influenza virus A/Memphis/1/71 (H3N2) is inhibited by sulphatide. A/Memphis/1/71 (H3N2) causes obvious haemagglutination and low-pH haemolysis of asialoerythrocytes reconstituted with sulphatide. All influenza A virus isolates from the species of animals so far tested bound to sulphatide. The sulphatide-binding specificity of the isolates was different from the viral sialyl-linkage specificity. Influenza A virus isolates also bound to galactosyl ceramide (GalCer; Gal beta 1 --> 1'Cer), as well as sulphatide, in the virus overlay assays. In contrast. the influenza virus did not bind to N-deacyl, a derivative of sulphatide, glucosyl ceramide or the other neutral glycolipids tested. These results indicate that the linkage of galactose, or sulphated galactose, to ceramide is important for viral binding.