tetano
Editor, Senior Moderator
Cell Host Microbe. 2016 Dec 14. pii: S1931-3128(16)30479-6. doi: 10.1016/j.chom.2016.11.004. [Epub ahead of print]
[h=1]Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.[/h] Peng W[SUP]1[/SUP], de Vries RP[SUP]1[/SUP], Grant OC[SUP]2[/SUP], Thompson AJ[SUP]1[/SUP], McBride R[SUP]1[/SUP], Tsogtbaatar B[SUP]1[/SUP], Lee PS[SUP]3[/SUP], Razi N[SUP]1[/SUP], Wilson IA[SUP]4[/SUP], Woods RJ[SUP]2[/SUP], Paulson JC[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] 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]
[h=1]Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.[/h] Peng W[SUP]1[/SUP], de Vries RP[SUP]1[/SUP], Grant OC[SUP]2[/SUP], Thompson AJ[SUP]1[/SUP], McBride R[SUP]1[/SUP], Tsogtbaatar B[SUP]1[/SUP], Lee PS[SUP]3[/SUP], Razi N[SUP]1[/SUP], Wilson IA[SUP]4[/SUP], Woods RJ[SUP]2[/SUP], Paulson JC[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] 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]