Tweet
Cell Host Microbe. 2016 Dec 14. pii: S1931-3128(16)30479-6. doi: 10.1016/j.chom.2016.11.004. [Epub ahead of print]
Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.
Peng W1, de Vries RP1, Grant OC2, Thompson AJ1, McBride R1, Tsogtbaatar B1, Lee PS3, Razi N1, Wilson IA4, Woods RJ2, Paulson JC5.
Author information
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.
Copyright ? 2016 Elsevier Inc. All rights reserved.
KEYWORDS:
H3N2; airway; bidentate binding; chemo-enzymatic synthesis; extended branched glycans; hemagglutinin; influenza virus; poly-N-acetyl-lactosamine; receptor specificity; sialoside microarray
PMID: 28017661 DOI: 10.1016/j.chom.2016.11.004
[PubMed - as supplied by publisher]
Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.
Peng W1, de Vries RP1, Grant OC2, Thompson AJ1, McBride R1, Tsogtbaatar B1, Lee PS3, Razi N1, Wilson IA4, Woods RJ2, Paulson JC5.
Author information
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.
Copyright ? 2016 Elsevier Inc. All rights reserved.
KEYWORDS:
H3N2; airway; bidentate binding; chemo-enzymatic synthesis; extended branched glycans; hemagglutinin; influenza virus; poly-N-acetyl-lactosamine; receptor specificity; sialoside microarray
PMID: 28017661 DOI: 10.1016/j.chom.2016.11.004
[PubMed - as supplied by publisher]