5E64

Hemagglutinin-esterase-fusion protein structure of influenza D virus

Summary for 5E64

• Entry DOI: 10.2210/pdb5e64/pdb
• Related: 5E5W 5E62 5E65 5E66
• Descriptor: Hemagglutinin-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 Keywords: influenza virus, hef, surface, hydrolase
• Biological source: Influenza D virus (D/swine/Oklahoma/1334/2011); More
• Total number of polymer chains: 4
• Total formula weight: 134248.46

Authors

Song, H.,Qi, J.,Shi, Y.,Gao, G.F. (deposition date: 2015-10-09, release date: 2016-03-23, Last modification date: 2024-11-13)

Primary citation

Song, 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

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)