tetano
Editor, Senior Moderator
J Biol Chem. 2014 Aug 18. pii: jbc.M114.588541. [Epub ahead of print]
Glycomic characterisation of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studies.
Jia N1, Barclay WS1, Roberts K1, Yen HL2, Chan RW2, Lam AK3, Air G4, Peiris JM2, Dell A1, Nicholls JM2, Haslam SM5.
Author information
Abstract
The initial recognition between influenza virus and 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 characterisation of respiratory tissues of ferret which allows a comparison of potential viral receptors to be made between human and ferret. To complement the structural analysis, lectin staining experiments were performed to characterise the regional distributions of glycans along the respiratory tract of ferret. Lastly, the binding between glycans identified and hemagglutinins of different strains of influenza viruses were 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 LacdiNAc (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.
Copyright ? 2014, The American Society for Biochemistry and Molecular Biology.
KEYWORDS:
carbohydrate structure; glycomics; influenza virus; mass spectrometry (MS); sialic acid
PMID:
25135641
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25135641
Glycomic characterisation of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studies.
Jia N1, Barclay WS1, Roberts K1, Yen HL2, Chan RW2, Lam AK3, Air G4, Peiris JM2, Dell A1, Nicholls JM2, Haslam SM5.
Author information
Abstract
The initial recognition between influenza virus and 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 characterisation of respiratory tissues of ferret which allows a comparison of potential viral receptors to be made between human and ferret. To complement the structural analysis, lectin staining experiments were performed to characterise the regional distributions of glycans along the respiratory tract of ferret. Lastly, the binding between glycans identified and hemagglutinins of different strains of influenza viruses were 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 LacdiNAc (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.
Copyright ? 2014, The American Society for Biochemistry and Molecular Biology.
KEYWORDS:
carbohydrate structure; glycomics; influenza virus; mass spectrometry (MS); sialic acid
PMID:
25135641
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25135641