tetano
Editor, Senior Moderator
Nat Commun
. 2022 Jul 13;13(1):4054.
doi: 10.1038/s41467-022-31840-0.
Human-type sialic acid receptors contribute to avian influenza A virus binding and entry by hetero-multivalent interactions
Mengying Liu[SUP] 1 [/SUP], Liane Z X Huang[SUP] 1 [/SUP], Anthony A Smits[SUP] 1 [/SUP], Christian Büll[SUP] 2 3 [/SUP], Yoshiki Narimatsu[SUP] 2 [/SUP], Frank J M van Kuppeveld[SUP] 1 [/SUP], Henrik Clausen[SUP] 2 [/SUP], Cornelis A M de Haan[SUP] 4 [/SUP], Erik de Vries[SUP] 5 [/SUP]
Affiliations
Abstract
Establishment of zoonotic viruses, causing pandemics like the Spanish flu and Covid-19, requires adaptation to human receptors. Pandemic influenza A viruses (IAV) that crossed the avian-human species barrier switched from binding avian-type α2-3-linked sialic acid (2-3Sia) to human-type 2-6Sia receptors. Here, we show that this specificity switch is however less dichotomous as generally assumed. Binding and entry specificity were compared using mixed synthetic glycan gradients of 2-3Sia and 2-6Sia and by employing a genetically remodeled Sia repertoire on the surface of a Sia-free cell line and on a sialoglycoprotein secreted from these cells. Expression of a range of (mixed) 2-3Sia and 2-6Sia densities shows that non-binding human-type receptors efficiently enhanced avian IAV binding and entry provided the presence of a low density of high affinity avian-type receptors, and vice versa. Considering the heterogeneity of sialoglycan receptors encountered in vivo, hetero-multivalent binding is physiologically relevant and will impact evolutionary pathways leading to host adaptation.
. 2022 Jul 13;13(1):4054.
doi: 10.1038/s41467-022-31840-0.
Human-type sialic acid receptors contribute to avian influenza A virus binding and entry by hetero-multivalent interactions
Mengying Liu[SUP] 1 [/SUP], Liane Z X Huang[SUP] 1 [/SUP], Anthony A Smits[SUP] 1 [/SUP], Christian Büll[SUP] 2 3 [/SUP], Yoshiki Narimatsu[SUP] 2 [/SUP], Frank J M van Kuppeveld[SUP] 1 [/SUP], Henrik Clausen[SUP] 2 [/SUP], Cornelis A M de Haan[SUP] 4 [/SUP], Erik de Vries[SUP] 5 [/SUP]
Affiliations
- PMID: 35831293
- DOI: 10.1038/s41467-022-31840-0
Abstract
Establishment of zoonotic viruses, causing pandemics like the Spanish flu and Covid-19, requires adaptation to human receptors. Pandemic influenza A viruses (IAV) that crossed the avian-human species barrier switched from binding avian-type α2-3-linked sialic acid (2-3Sia) to human-type 2-6Sia receptors. Here, we show that this specificity switch is however less dichotomous as generally assumed. Binding and entry specificity were compared using mixed synthetic glycan gradients of 2-3Sia and 2-6Sia and by employing a genetically remodeled Sia repertoire on the surface of a Sia-free cell line and on a sialoglycoprotein secreted from these cells. Expression of a range of (mixed) 2-3Sia and 2-6Sia densities shows that non-binding human-type receptors efficiently enhanced avian IAV binding and entry provided the presence of a low density of high affinity avian-type receptors, and vice versa. Considering the heterogeneity of sialoglycan receptors encountered in vivo, hetero-multivalent binding is physiologically relevant and will impact evolutionary pathways leading to host adaptation.