Analysis of <Emphasis Type="Italic">N</Emphasis>-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses |
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| Authors: | Nongluk Sriwilaijaroen Sachiko Kondo Hirokazu Yagi Prapon Wilairat Hiroaki Hiramatsu Morihiro Ito Yasuhiko Ito Koichi Kato |
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| Institution: | (1) Present address: Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, 1200 Matsumoto-cho, Kasugai Aichi, 487-8501, Japan;(2) Faculty of Medicine, Thammasat University, Rangsit Campus, Pathumthani, 12120, Thailand;(3) Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan;(4) GLYENCE Co., Ltd., 2-22-8 Chikusa, Chikusa-ku, Nagoya 464-0858, Japan;(5) CREST, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Japan;(6) Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand;(7) The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan;(8) Institute for Molecular Science National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan;(9) Global COE Program for Innovation in Human Health Sciences, University of Shizuoka School of Pharmaceutical Sciences, 52-1 Yada, Shizuoka 422-8526, Japan; |
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| Abstract: | The initial step essential in influenza virus infection is specific binding of viral hemagglutinin to host cell-surface glycan
receptors. Influenza A virus specificity for the host is mediated by viral envelope hemagglutinin, that binds to receptors
containing glycans with terminal sialic acids. Human viruses preferentially bind to α2→6 linked sialic acids on receptors
of host cells, whereas avian viruses are specific for the α2→3 linkage on the target cells. Human influenza virus isolates
more efficiently infect amniotic membrane (AM) cells than chorioallantoic membrane (CAM) cells. N-glycans were isolated from AM and CAM cells of 10-day-old chicken embryonated eggs and their structures were analyzed by
multi-dimensional HPLC mapping and MALDI-TOF-MS techniques. Terminal N-acetylneuraminic acid contents in the two cell types were similar. However, molar percents of α2→3 linkage preferentially
bound by avian influenza virus were 27.2 in CAM cells and 15.4 in AM cells, whereas those of α2→6 linkage favored by human
influenza virus were 8.3 (CAM) and 14.2 (AM). Molar percents of sulfated glycans, recognized by human influenza virus, in
CAM and AM cells were 3.8 and 12.7, respectively. These results have revealed structures and molar percents of N-glycans in CAM and AM cells important in determining human and avian influenza virus infection and viral adaptation. |
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| Keywords: | Influenza virus N-glycans HPLC-MALDI-TOF mapping Chorioallantoic membrane Amniotic membrane Host cell receptor specificity |
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