4H32

The crystal structure of the hemagglutinin H17 derived the bat influenza A virus

Summary for 4H32

• Entry DOI: 10.2210/pdb4h32/pdb
• Descriptor: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: homotrimer, virus entry and fusion, envelope of virus, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 12
• Total formula weight: 335608.82

Authors

Sun, X.,Shi, Y.,Lu, X.,He, J.,Gao, F.,Yan, J.,Qi, J.,Gao, G.F. (deposition date: 2012-09-13, release date: 2013-07-10, Last modification date: 2024-10-30)

Primary citation

Sun, X.,Shi, Y.,Lu, X.,He, J.,Gao, F.,Yan, J.,Qi, J.,Gao, G.F.
Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism.
Cell Rep, 3:769-778, 2013

PubMed Abstract: A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 Å resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human α2,6 SA-linkage or avian α2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.

PubMed: 23434510
DOI: 10.1016/j.celrep.2013.01.025

Experimental method

X-RAY DIFFRACTION (2.7 Å)