Abstract
Human and avian influenza viruses recognize different sialic acid-containing receptors, referred to as human-type (NeuAcα2-6Gal) and avian-type (NeuAcα2-3Gal), respectively. This presents a species barrier for aerosol droplet transmission of avian viruses in humans and ferrets. Recent reports have suggested that current human H3N2 viruses no longer have strict specificity toward human-type receptors. Using an influenza receptor glycan microarray with extended airway glycans, we find that H3N2 viruses have in fact maintained human-type specificity, but they have evolved preference for a subset of receptors comprising branched glycans with extended poly-N-acetyl-lactosamine (poly-LacNAc) chains, a specificity shared with the 2009 pandemic H1N1 (Cal/04) hemagglutinin. Lipid-linked versions of extended sialoside receptors can restore susceptibility of sialidase-treated MDCK cells to infection by both recent (A/Victoria/361/11) and historical (A/Hong Kong/8/1968) H3N2 viruses. Remarkably, these human-type receptors with elongated branches have the potential to increase avidity by simultaneously binding to two subunits of a single hemagglutinin trimer.
Original language | English |
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Pages (from-to) | 23-34 |
Number of pages | 12 |
Journal | Cell Host and Microbe |
Volume | 21 |
Issue number | 1 |
DOIs | |
Publication status | Published - 11 Jan 2017 |
Keywords
- influenza virus
- H3N2
- hemagglutinin
- receptor specificity
- airway
- chemo-enzymatic synthesis
- sialoside microarray
- extended branched glycans
- poly-N-acetyl-lactosamine
- bidentate binding