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Article: Glycomic characterization of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studies

TitleGlycomic characterization of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studies
Authors
Issue Date2014
Citation
Journal of Biological Chemistry, 2014, v. 289 n. 41, p. 28489-28504 How to Cite?
AbstractThe initial recognition between influenza virus and the host cell is mediated by interactions between the viral surface protein hemagglutinin and sialic acid-terminated glycoconjugates on the host cell surface. The sialic acid residues can be linked to the adjacent monosaccharide by α2-3- or α2-6-type glycosidic bonds. It is this linkage difference that primarily defines the species barrier of the influenza virus infection with α2-3 binding being associated with avian influenza viruses and α2-6 binding being associated with human strains. The ferret has been extensively used as an animal model to study the transmission of influenza. To better understand the validity of this model system, we undertook glycomic characterization of respiratory tissues of ferret, which allows a comparison of potential viral receptors to be made between humans and ferrets. To complement the structural analysis, lectin staining experiments were performed to characterize the regional distributions of glycans along the respiratory tract of ferrets. Finally, the binding between the glycans identified and the hemagglutinins of different strains of influenza viruses was assessed by glycan array experiments. Our data indicated that the respiratory tissues of ferret heterogeneously express both α2-3- and α2-6-linked sialic acids. However, the respiratory tissues of ferret also expressed the Sda epitope (NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcNAc) and sialylated N,N'-diacetyllactosamine (NeuAcα2-6GalNAcβ1-4GlcNAc), which have not been observed in the human respiratory tract surface epithelium. The presence of the Sda epitope reduces potential binding sites for avian viruses and thus may have implications for the usefulness of the ferret in the study of influenza virus infection.
Persistent Identifierhttp://hdl.handle.net/10722/207838
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorJia, Nen_US
dc.contributor.authorBarclay, WSen_US
dc.contributor.authorRoberts, Ken_US
dc.contributor.authorYen, Hen_US
dc.contributor.authorChan, WYen_US
dc.contributor.authorLam, AKen_US
dc.contributor.authorAir, Gen_US
dc.contributor.authorPeiris, JSMen_US
dc.contributor.authorDell, Aen_US
dc.contributor.authorNicholls, JMen_US
dc.contributor.authorHaslam, SMen_US
dc.date.accessioned2015-01-19T11:23:03Z-
dc.date.available2015-01-19T11:23:03Z-
dc.date.issued2014en_US
dc.identifier.citationJournal of Biological Chemistry, 2014, v. 289 n. 41, p. 28489-28504en_US
dc.identifier.urihttp://hdl.handle.net/10722/207838-
dc.description.abstractThe initial recognition between influenza virus and the host cell is mediated by interactions between the viral surface protein hemagglutinin and sialic acid-terminated glycoconjugates on the host cell surface. The sialic acid residues can be linked to the adjacent monosaccharide by α2-3- or α2-6-type glycosidic bonds. It is this linkage difference that primarily defines the species barrier of the influenza virus infection with α2-3 binding being associated with avian influenza viruses and α2-6 binding being associated with human strains. The ferret has been extensively used as an animal model to study the transmission of influenza. To better understand the validity of this model system, we undertook glycomic characterization of respiratory tissues of ferret, which allows a comparison of potential viral receptors to be made between humans and ferrets. To complement the structural analysis, lectin staining experiments were performed to characterize the regional distributions of glycans along the respiratory tract of ferrets. Finally, the binding between the glycans identified and the hemagglutinins of different strains of influenza viruses was assessed by glycan array experiments. Our data indicated that the respiratory tissues of ferret heterogeneously express both α2-3- and α2-6-linked sialic acids. However, the respiratory tissues of ferret also expressed the Sda epitope (NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcNAc) and sialylated N,N'-diacetyllactosamine (NeuAcα2-6GalNAcβ1-4GlcNAc), which have not been observed in the human respiratory tract surface epithelium. The presence of the Sda epitope reduces potential binding sites for avian viruses and thus may have implications for the usefulness of the ferret in the study of influenza virus infection.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.titleGlycomic characterization of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studiesen_US
dc.typeArticleen_US
dc.identifier.emailYen, H: hyen@hku.hken_US
dc.identifier.emailChan, WY: reneewy@hku.hken_US
dc.identifier.emailPeiris, JSM: malik@hkucc.hku.hken_US
dc.identifier.emailNicholls, JM: jmnichol@hkucc.hku.hken_US
dc.identifier.authorityYen, H=rp00304en_US
dc.identifier.authorityChan, WY=rp01596en_US
dc.identifier.authorityPeiris, JSM=rp00410en_US
dc.identifier.authorityNicholls, JM=rp00364en_US
dc.identifier.doi10.1074/jbc.M114.588541en_US
dc.identifier.pmcidPMC4192499-
dc.identifier.hkuros242085en_US
dc.identifier.volume289en_US
dc.identifier.issue41en_US
dc.identifier.spage28489en_US
dc.identifier.epage28504en_US

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