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

• Published in: Biochemical journal 1996-09, Vol.318 ( Pt 2) (2), p.389-393
• Main Authors: Suzuki, T, Sometani, A, Yamazaki, Y, Horiike, G, Mizutani, Y, Masuda, H, Yamada, M, Tahara, H, Xu, G, Miyamoto, D, Oku, N, Okada, S, Kiso, M, Hasegawa, A, Ito, T, Kawaoka, Y, Suzuki, Y
• Format: Article
• Language: English
• Subjects: Animals; Carbohydrate Conformation; Carbohydrate Sequence; Cell Line; Ceramides - chemistry; Ceramides - metabolism; Ceramides - pharmacology; Dogs; Erythrocytes - drug effects; Erythrocytes - physiology; Erythrocytes - virology; Glycolipids - pharmacology; Hemagglutination Tests; Humans; influenza A virus; Influenza A virus - drug effects; Influenza A virus - physiology; Kidney; Molecular Sequence Data; Sulfoglycosphingolipids - chemistry; Sulfoglycosphingolipids - metabolism; Sulfoglycosphingolipids - pharmacology; Virus Replication - drug effects
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj3180389

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.