We found, by using a virus overlay assay, that influenza A virus isolates bind to sulphatide (HSO3-Galβ1 → 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; Galβ1 → 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.
Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection
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Takashi SUZUKI, Ayako SOMETANI, Yasuhiro YAMAZAKI, Goh HORIIKE, Yukiko MIZUTANI, Hiroyuki MASUDA, Mika YAMADA, Harunobu TAHARA, Guiyun XU, Daisei MIYAMOTO, Naoto OKU, Shoji OKADA, Makoto KISO, Akira HASEGAWA, Toshihiro ITO, Yoshihiro KAWAOKA, Yasuo SUZUKI; Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection. Biochem J 1 September 1996; 318 (2): 389–393. doi: https://doi.org/10.1042/bj3180389
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