Date Published: March 14, 2013
Publisher: Public Library of Science
Author(s): Trevenan Walther, Rositsa Karamanska, Renee W. Y. Chan, Michael C. W. Chan, Nan Jia, Gillian Air, Clark Hopton, Maria P. Wong, Anne Dell, J. S. Malik Peiris, Stuart M. Haslam, John M. Nicholls, Andrew Pekosz.
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.
Influenza virus infection in humans presents an economic and social health burden to society. Yearly infections are normally due to H1N1, H3N2 or influenza B strains while pandemics occur at 30–40 year intervals due to antigenic shift or the emergence of new strains, such as the introduction of H1N1 of swine origin into the human population which occurred in 2009.