tetano
Editor, Senior Moderator
PLoS Pathog. 2013 Mar;9(3):e1003223. doi: 10.1371/journal.ppat.1003223. Epub 2013 Mar 14.
Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection.
Walther T, Karamanska R, Chan RW, Chan MC, Jia N, Air G, Hopton C, Wong MP, Dell A, Malik Peiris JS, Haslam SM, Nicholls JM.
Source
Department of Pathology, The University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, China.
Abstract
The first step in influenza infection of the human respiratory tract is binding of the virus to sialic (Sia) acid terminated receptors. The binding of different strains of virus for the receptor is determined by the α linkage of the sialic acid to galactose and the adjacent glycan structure. In this study the N- and O-glycan composition of the human lung, bronchus and nasopharynx was characterized by mass spectrometry. Analysis showed that there was a wide spectrum of both Sia α2-3 and α2-6 glycans in the lung and bronchus. This glycan structural data was then utilized in combination with binding data from 4 of the published glycan arrays to assess whether these current glycan arrays were able to predict replication of human, avian and swine viruses in human ex vivo respiratory tract tissues. The most comprehensive array from the Consortium for Functional Glycomics contained the greatest diversity of sialylated glycans, but was not predictive of productive replication in the bronchus and lung. Our findings indicate that more comprehensive but focused arrays need to be developed to investigate influenza virus binding in an assessment of newly emerging influenza viruses.
PMID:
23516363
[PubMed - in process]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/23516363
Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection.
Walther T, Karamanska R, Chan RW, Chan MC, Jia N, Air G, Hopton C, Wong MP, Dell A, Malik Peiris JS, Haslam SM, Nicholls JM.
Source
Department of Pathology, The University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, China.
Abstract
The first step in influenza infection of the human respiratory tract is binding of the virus to sialic (Sia) acid terminated receptors. The binding of different strains of virus for the receptor is determined by the α linkage of the sialic acid to galactose and the adjacent glycan structure. In this study the N- and O-glycan composition of the human lung, bronchus and nasopharynx was characterized by mass spectrometry. Analysis showed that there was a wide spectrum of both Sia α2-3 and α2-6 glycans in the lung and bronchus. This glycan structural data was then utilized in combination with binding data from 4 of the published glycan arrays to assess whether these current glycan arrays were able to predict replication of human, avian and swine viruses in human ex vivo respiratory tract tissues. The most comprehensive array from the Consortium for Functional Glycomics contained the greatest diversity of sialylated glycans, but was not predictive of productive replication in the bronchus and lung. Our findings indicate that more comprehensive but focused arrays need to be developed to investigate influenza virus binding in an assessment of newly emerging influenza viruses.
PMID:
23516363
[PubMed - in process]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/23516363