Publication: Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses
Issued Date
2009-05-01
Resource Type
ISSN
15734986
02820080
02820080
Other identifier(s)
2-s2.0-64149092513
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Mahidol University
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SCOPUS
Bibliographic Citation
Glycoconjugate Journal. Vol.26, No.4 (2009), 433-443
Suggested Citation
Nongluk Sriwilaijaroen, Sachiko Kondo, Hirokazu Yagi, Prapon Wilairat, Hiroaki Hiramatsu, Morihiro Ito, Yasuhiko Ito, Koichi Kato, Yasuo Suzuki Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses. Glycoconjugate Journal. Vol.26, No.4 (2009), 433-443. doi:10.1007/s10719-008-9193-x Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/27241
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Title
Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses
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.