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

5BQY

Crystal structure of hemagglutinin of A/Chicken/Guangdong/S1311/2010 (H6N6) in complex with avian-like receptor LSTa

Summary for 5BQY
Entry DOI10.2210/pdb5bqy/pdb
Related5BNY 5BQZ 5BR0 5BR3 5BR6
Related PRD IDPRD_900017
DescriptorHEMAGGLUTININ HA1 CHAIN, HEMAGGLUTININ HA2 CHAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsinfluenza, heamgglutinin, viral protein
Biological sourceInfluenza A virus (A/chicken/Guangdong/S1312/2010(H6N2))
More
Total number of polymer chains6
Total formula weight179977.99
Authors
Ni, F.,Kondrashkina, E.,Wang, Q. (deposition date: 2015-05-29, release date: 2015-08-12, Last modification date: 2024-10-09)
Primary citationNi, F.,Kondrashkina, E.,Wang, Q.
Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin.
Plos One, 7:e0134576-e0134576, 2015
Cited by
PubMed Abstract: In June 2013, the first human infection by avian influenza A(H6N1) virus was reported in Taiwan. This incident raised the concern for possible human epidemics and pandemics from H6 viruses. In this study, we performed structural and functional investigation on the hemagglutinin (HA) proteins of the human-infecting A/Taiwan/2/2013(H6N1) (TW H6) virus and an avian A/chicken/Guangdong/S1311/2010(H6N6) (GD H6) virus that transmitted efficiently in guinea pigs. Our results revealed that in the presence of HA1 Q226, the triad of HA1 S137, E190 and G228 in GD H6 HA allows the binding to both avian- and human-like receptors with a slight preference for avian receptors. Its conservation among the majority of H6 HAs provides an explanation for the broader host range of this subtype. Furthermore, the triad of N137, V190 and S228 in TW H6 HA may alleviate the requirement for a hydrophobic residue at HA1 226 of H2 and H3 HAs when binding to human-like receptors. Consequently, TW H6 HA has a slight preference for human receptors, thus may represent an intermediate towards a complete human adaptation. Importantly, the triad observed in TW H6 HA is detected in 74% H6 viruses isolated from Taiwan in the past 14 years, suggesting an elevated threat of H6 viruses from this region to human health. The novel roles of the triad at HA1 137, 190 and 228 of H6 HA in binding to receptors revealed here may also be used by other HA subtypes to achieve human adaptation, which needs to be further tested in laboratory and closely monitored in field surveillance.
PubMed: 26226046
DOI: 10.1371/journal.pone.0134576
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.78 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon