6IDD

Crystal structure of H7 hemagglutinin mutant SH1-AVPL ( S138A, G186V, T221P, Q226L) from the influenza virus A/Shanghai/1/2013 (H7N9)

Summary for 6IDD

• Entry DOI: 10.2210/pdb6idd/pdb
• Descriptor: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: influenza virus, h7n9, hemagglutinin, viral protein
• Biological source: Influenza A virus (A/Shanghai/MH01/2013(H7N9))
• Total number of polymer chains: 6
• Total formula weight: 334738.57

Authors

Gao, G.F.,Xu, Y.,Qi, J.X. (deposition date: 2018-09-09, release date: 2019-11-27, Last modification date: 2024-10-23)

Primary citation

Xu, Y.,Peng, R.,Zhang, W.,Qi, J.,Song, H.,Liu, S.,Wang, H.,Wang, M.,Xiao, H.,Fu, L.,Fan, Z.,Bi, Y.,Yan, J.,Shi, Y.,Gao, G.F.
Avian-to-Human Receptor-Binding Adaptation of Avian H7N9 Influenza Virus Hemagglutinin.
Cell Rep, 29:2217-, 2019

PubMed Abstract: Since 2013, H7N9 avian influenza viruses (AIVs) have caused more than 1,600 human infections, posing a threat to public health. An emerging concern is whether H7N9 AIVs will cause pandemics among humans. Molecular analysis of hemagglutinin (HA), which is a critical determinant of interspecies transmission, shows that the current H7N9 AIVs are still dual-receptor tropic, indicating limited human-to-human transmission potency. Mutagenesis and structural studies reveal that a G186V substitution is sufficient for H7N9 AIVs to acquire human receptor-binding capacity, and a Q226L substitution would favor binding to both avian and human receptors only when paired with A138/V186/P221 hydrophobic residues. These data suggest a different evolutionary route of H7N9 viruses compared to other AIV-subtype HAs.

PubMed: 31747596
DOI: 10.1016/j.celrep.2019.10.047

Experimental method

X-RAY DIFFRACTION (2.383 Å)