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8XR7

Dual receptor-binding, infectivity, and transmissibility of an emerging H2N2 avian influenza virus

Summary for 8XR7
Entry DOI10.2210/pdb8xr7/pdb
EMDB information38597
DescriptorHemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordsh2n2, influenza virus, receptor, replication, transmission, mice, guinea pig, ferret, mutation, public health risk, virus, viral protein
Biological sourceInfluenza A virus (strain A/Korea/426/1968 H2N2)
Total number of polymer chains3
Total formula weight171400.27
Authors
Sun, J.,Zheng, T.Y. (deposition date: 2024-01-06, release date: 2025-01-15)
Primary citationSun, J.,Zheng, T.,Jia, M.,Wang, Y.,Yang, J.,Liu, Y.,Yang, P.,Xie, Y.,Sun, H.,Tong, Q.,Li, J.,Yang, J.,Fu, G.,Shi, Y.,Qi, J.,Liu, W.,Liu, J.,Tian, W.X.,Gao, G.F.,Bi, Y.
Dual receptor-binding, infectivity, and transmissibility of an emerging H2N2 low pathogenicity avian influenza virus.
Nat Commun, 15:10012-10012, 2024
Cited by
PubMed Abstract: The 1957 H2N2 influenza pandemic virus [A(H2N2)pdm1957] has disappeared from humans since 1968, while H2N2 avian influenza viruses (AIVs) are still circulating in birds. It is necessary to reveal the recurrence risk and potential cross-species infection of these AIVs from avian to mammals. We find that H2 AIVs circulating in domestic poultry in China have genetic and antigenic differences compared to the A(H2N2)pdm1957. One H2N2 AIV has a dual receptor-binding property similar to that of the A(H2N2)pdm1957. Molecular and structural studies reveal that the N144S, and N144E or R137M substitutions in hemagglutinin (HA) enable H2N2 avian or human viruses to bind or preferentially bind human-type receptor. The H2N2 AIV rapidly adapts to mice (female) and acquires mammalian-adapted mutations that facilitated transmission in guinea pigs and ferrets (female). These findings on the receptor-binding, infectivity, transmission, and mammalian-adaptation characteristics of H2N2 AIVs provide a reference for early-warning and prevention for this subtype.
PubMed: 39562538
DOI: 10.1038/s41467-024-54374-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.62 Å)
Structure validation

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