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5E66

The complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-N-Ac-Sia

Summary for 5E66
Entry DOI10.2210/pdb5e66/pdb
Related5E5W 5E62 5E64 5E65
DescriptorHemagglutinin-esterase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordsinfluenza, complex, hef, hydrolase
Biological sourceInfluenza D virus (D/swine/Oklahoma/1334/2011)
More
Total number of polymer chains2
Total formula weight67500.59
Authors
Song, H.,Qi, J.,Shi, Y.,Gao, G.F. (deposition date: 2015-10-09, release date: 2016-03-23, Last modification date: 2024-11-06)
Primary citationSong, H.,Qi, J.,Khedri, Z.,Diaz, S.,Yu, H.,Chen, X.,Varki, A.,Shi, Y.,Gao, G.F.
An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism
PLoS Pathog., 12:e1005411-e1005411, 2016
Cited by
PubMed Abstract: 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.
PubMed: 26816272
DOI: 10.1371/journal.ppat.1005411
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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数据于2024-11-06公开中

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