tetano
Editor, Senior Moderator
PLoS Pathog. 2016 Jan 27;12(1):e1005411. doi: 10.1371/journal.ppat.1005411. eCollection 2016.
[h=1]An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.[/h] Song H[SUP]1,[/SUP][SUP]2[/SUP], Qi J[SUP]1[/SUP], Khedri Z[SUP]3[/SUP], Diaz S[SUP]3[/SUP], Yu H[SUP]4[/SUP], Chen X[SUP]4[/SUP], Varki A[SUP]4[/SUP], Shi Y[SUP]1,[/SUP][SUP]2,[/SUP][SUP]5[/SUP], Gao GF[SUP]1,[/SUP][SUP]2,[/SUP][SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.
PMID: 26816272 [PubMed - in process] Free full text
[h=1]An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.[/h] Song H[SUP]1,[/SUP][SUP]2[/SUP], Qi J[SUP]1[/SUP], Khedri Z[SUP]3[/SUP], Diaz S[SUP]3[/SUP], Yu H[SUP]4[/SUP], Chen X[SUP]4[/SUP], Varki A[SUP]4[/SUP], Shi Y[SUP]1,[/SUP][SUP]2,[/SUP][SUP]5[/SUP], Gao GF[SUP]1,[/SUP][SUP]2,[/SUP][SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.
PMID: 26816272 [PubMed - in process] Free full text