Open Glycoscience

2012, 5 : 2-12
Published online 2012 May 4. DOI: 10.2174/1875398101205010002
Publisher ID: TOGLYJ-5-2

Comparative Analyses of N-Glycosylation Profiles of Influenza A Viruses Grown in Different Host Cells

Hirokazu Yagi , Shinya Watanabe , Takashi Suzuki , Tadanobu Takahashi , Yasuo Suzuki and Koichi Kato
Graduate School of Pharma-ceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.

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.

Keywords:

Influenza virus A / N-glycans / HPLC mapping / host specific glycosylation.