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5VJK

Crystal structure of H7 hemagglutinin mutant (V186K, K193T, G228S) from the influenza virus A/Shanghai/2/2013 (H7N9)

Summary for 5VJK
Entry DOI10.2210/pdb5vjk/pdb
Related5VJL 5VJM
DescriptorHemagglutinin HA1, Hemagglutinin HA2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsinfluenza virus, hemagglutinin, mutant, receptor specificity, viral protein
Biological sourceInfluenza A virus
More
Total number of polymer chains2
Total formula weight57476.06
Authors
Zhu, X.,Wilson, I.A. (deposition date: 2017-04-19, release date: 2017-05-24, Last modification date: 2024-11-13)
Primary citationde Vries, R.P.,Peng, W.,Grant, O.C.,Thompson, A.J.,Zhu, X.,Bouwman, K.M.,de la Pena, A.T.T.,van Breemen, M.J.,Ambepitiya Wickramasinghe, I.N.,de Haan, C.A.M.,Yu, W.,McBride, R.,Sanders, R.W.,Woods, R.J.,Verheije, M.H.,Wilson, I.A.,Paulson, J.C.
Three mutations switch H7N9 influenza to human-type receptor specificity.
PLoS Pathog., 13:e1006390-e1006390, 2017
Cited by
PubMed Abstract: The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry. The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses. While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans. To determine if the H7 HA was capable of acquiring human-type receptor specificity, we conducted mutation analyses. Remarkably, three amino acid mutations conferred a switch in specificity for human-type receptors that resembled the specificity of the 2009 human H1 pandemic virus, and promoted binding to human trachea epithelial cells.
PubMed: 28617868
DOI: 10.1371/journal.ppat.1006390
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.593 Å)
Structure validation

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