tetano
Editor, Senior Moderator
Vet Res. 2017 Feb 6;48(1):7. doi: 10.1186/s13567-017-0410-0.
[h=1]The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs.[/h] Gu M[SUP]1,[/SUP][SUP]2[/SUP], Li Q[SUP]1[/SUP], Gao R[SUP]1[/SUP], He D[SUP]1[/SUP], Xu Y[SUP]1[/SUP], Xu H[SUP]1[/SUP], Xu L[SUP]1,[/SUP][SUP]3[/SUP], Wang X[SUP]1,[/SUP][SUP]2[/SUP], Hu J[SUP]1,[/SUP][SUP]2[/SUP], Liu X[SUP]1,[/SUP][SUP]2[/SUP], Hu S[SUP]1,[/SUP][SUP]2[/SUP], Peng D[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP], Jiao X[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP], Liu X[SUP]5,[/SUP][SUP]6,[/SUP][SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to α-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both α-2,3 (avian-type) and α-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.
PMID: 28166830 PMCID: PMC5294818 DOI: 10.1186/s13567-017-0410-0
[PubMed - in process] Free full text
[h=1]The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs.[/h] Gu M[SUP]1,[/SUP][SUP]2[/SUP], Li Q[SUP]1[/SUP], Gao R[SUP]1[/SUP], He D[SUP]1[/SUP], Xu Y[SUP]1[/SUP], Xu H[SUP]1[/SUP], Xu L[SUP]1,[/SUP][SUP]3[/SUP], Wang X[SUP]1,[/SUP][SUP]2[/SUP], Hu J[SUP]1,[/SUP][SUP]2[/SUP], Liu X[SUP]1,[/SUP][SUP]2[/SUP], Hu S[SUP]1,[/SUP][SUP]2[/SUP], Peng D[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP], Jiao X[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP], Liu X[SUP]5,[/SUP][SUP]6,[/SUP][SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to α-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both α-2,3 (avian-type) and α-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.
PMID: 28166830 PMCID: PMC5294818 DOI: 10.1186/s13567-017-0410-0
[PubMed - in process] Free full text