Affiliations: [a] Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, OK, USA | [b] Department of Biochemistry, Emory University, OK, USA | Biochemistry and Bio-related Chemistry Branch Pharmacology, Physiology, and Biological Chemistry Division NIGMS, NIH
Correspondence:
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Corresponding author: Gillian M. Air, Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, PO Box 26901, Oklahoma City, OK 73151, USA. Tel.: +1 405 271 2227; E-mail: [email protected].
Abstract: Influenza viruses initiate infection by attaching to sialic acid receptors on the surface of host cells. It has been recognized for some time that avian influenza viruses usually bind to terminal sialic acid that is linked in the α2-3 configuration to the next sugar while human viruses show preference for α2-6 linked sialic acid. With developments in synthetic chemistry and chemo-enzymatic methods of synthesizing quite complex glycans, it has become clear that the binding specificity extends beyond the sialic acid, and this has led to considerable interest in developing glycan reagents that could be used either as a diagnostic tool for particular influenza viruses, or to identify cells that are susceptible to infection by certain influenza viruses. Here we describe the use of the Consortium for Functional Glycomics Glycan Array to investigate binding specificity of influenza hemagglutinin and cleavage by neuraminidase, using seasonal and pandemic H1N1 influenza viruses as examples, and compare the results with published data using other array methods.
