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. 1996 Sep 1;318(Pt 2):389–393. doi: 10.1042/bj3180389

Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection.

T Suzuki 1, A Sometani 1, Y Yamazaki 1, G Horiike 1, Y Mizutani 1, H Masuda 1, M Yamada 1, H Tahara 1, G Xu 1, D Miyamoto 1, N Oku 1, S Okada 1, M Kiso 1, A Hasegawa 1, T Ito 1, Y Kawaoka 1, Y Suzuki 1
PMCID: PMC1217634  PMID: 8809024

Abstract

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.

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Selected References

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