Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity

Publication date: Available online 22 December 2016
Source:Cell Host & Microbe
Author(s): Wenjie Peng, Robert P. de Vries, Oliver C. Grant, Andrew J. Thompson, Ryan McBride, Buyankhishig Tsogtbaatar, Peter S. Lee, Nahid Razi, Ian A. Wilson, Robert J. Woods, James C. Paulson
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.

Graphical abstract

Teaser

To clarify H3N2 human influenza virus receptor specificity, Peng et al. developed a glycan array that included extended glycans. Recent H3N2 and 2009 pandemic H1N1 viruses share specificity for human-type receptors with extended glycan chains, conferring potential for increased avidity by simultaneously binding two subunits of a single hemagglutinin trimer.


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