title: Sulphatide binds to human and animal influenza A viruses, and inhibits the viral infection.
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.
authors.affiliation: Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
authors.forename: A
authors.initials: A
authors.lastname: Sometani
authors.forename: Y
authors.initials: Y
authors.lastname: Yamazaki
authors.forename: G
authors.initials: G
authors.lastname: Horiike
authors.forename: Y
authors.initials: Y
authors.lastname: Mizutani
authors.forename: H
authors.initials: H
authors.lastname: Masuda
authors.forename: M
authors.initials: M
authors.lastname: Yamada
authors.forename: H
authors.initials: H
authors.lastname: Tahara
authors.forename: G
authors.initials: G
authors.lastname: Xu
authors.forename: D
authors.initials: D
authors.lastname: Miyamoto
authors.forename: N
authors.initials: N
authors.lastname: Oku
authors.forename: S
authors.initials: S
authors.lastname: Okada
authors.forename: M
authors.initials: M
authors.lastname: Kiso
authors.forename: A
authors.initials: A
authors.lastname: Hasegawa
authors.forename: T
authors.initials: T
authors.lastname: Ito
authors.forename: Y
authors.initials: Y
authors.lastname: Kawaoka
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
mesh_terms: D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D002518:Ceramides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D004285:Dogs; D004912:Erythrocytes / Q000187:drug effects / Q000502:physiology / Q000821:virology; D006017:Glycolipids / Q000494:pharmacology; D006386:Hemagglutination Tests; D006801:Humans; D009980:Influenza A virus / Q000187:drug effects / Q000502:physiology*; D007668:Kidney; D008969:Molecular Sequence Data; D013433:Sulfoglycosphingolipids / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D014779:Virus Replication / Q000187:drug effects*
chemical_list: D002518:Ceramides; D006017:Glycolipids; D013433:Sulfoglycosphingolipids