Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5XL5

The structure of hemagglutinin Q226L mutant from an avian-origin H4N6 influenza virus

Summary for 5XL5
Entry DOI10.2210/pdb5xl5/pdb
DescriptorHemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsh4 hemagglutinin, influenza virus, receptor binding, viral protein
Biological sourceInfluenza A virus (strain A/Duck/Czechoslovakia/1956 H4N6)
More
Cellular locationHost apical cell membrane ; Single-pass type I membrane protein : A3KF09 A3KF09
Total number of polymer chains4
Total formula weight113472.59
Authors
Song, H.,Qi, J.,Gao, G.F. (deposition date: 2017-05-10, release date: 2017-08-02, Last modification date: 2024-10-23)
Primary citationSong, H.,Qi, J.,Xiao, H.,Bi, Y.,Zhang, W.,Xu, Y.,Wang, F.,Shi, Y.,Gao, G.F.
Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4
Cell Rep, 20:1201-1214, 2017
Cited by
PubMed Abstract: Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evidence shows that H4 subtype viruses have been widely circulating in domestic poultry and human asymptomatic infections might have occurred. Here, we evaluated the receptor-binding properties of two representative isolates, avian H4N6 (containing Q226 and G228) and swine H4N6 (containing L226 and S228), and found that the avian isolate preferentially binds to avian receptors, whereas the swine isolate preferentially binds to human receptors. The Q226L and G228S substitutions are pivotal for the receptor-binding switch, which resulted in similar human receptor-binding features to the pandemic H2 and H3, implying that H4 has the potential to cause human infections. This early-warning study calls for future extensive surveillance.
PubMed: 28768203
DOI: 10.1016/j.celrep.2017.07.028
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon