Abstract
Glycosylation of the surface glycoproteins of influenza A virus is associated with several viral properties such as receptor binding and susceptibility to neuraminidase inhibitors. In this study, we evaluated the detailed structures of N-glycans derived from the same influenza virus strain A/Memphis/1/71 (H3N2) grown in different host cells, i.e., Madin-Darby canine kidney (MDCK) cells and embryonated eggs. Although both influenza virus isolates expressed neu- tral and sulfated oligosaccharides, their detailed profiles were significantly different. In contrast, N-glycosylation profiles of the influenza virus isolate from MDCK cells were highly homologous with those of desialylated N-glycans derived from its host cells. These data demonstrate that the glycosylation of influenza viruses is governed by their host cells.
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