| Autor: |
SUZUKI, Takashi, SOMETANI, Ayako, YAMAZAKI, Yasuhiro, HORIIKE, Goh, MIZUTANI, Yukiko, MASUDA, Hiroyuki, YAMADA, Mika, TAHARA, Harunobu, XU, Guiyun, MIYAMOTO, Daisei, OKU, Naoto, OKADA, Shoji, KISO, Makoto, HASEGAWA, Akira, ITO, Toshihiro, KAWAOKA, Yoshihiro, SUZUKI, Yasuo |
| Zdroj: |
Biochemical Journal; September 1996, Vol. 318 Issue: 2 p389-393, 5p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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