3ZP2

INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTa

Summary for 3ZP2

• Entry DOI: 10.2210/pdb3zp2/pdb
• Related: 3ZP0 3ZP1 3ZP3 3ZP6 3ZPA 3ZPB
• Descriptor: HAEMAGGLUTININ, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: viral protein
• Biological source: INFLUENZA A VIRUS; More
• Total number of polymer chains: 2
• Total formula weight: 57074.81

Authors

Liu, J.,Stevens, D.J.,Gamblin, S.J.,Skehel, J.J. (deposition date: 2013-02-26, release date: 2013-10-02, Last modification date: 2024-10-23)

Primary citation

Crusat, M.,Liu, J.,Palma, A.S.,Childs, R.A.,Liu, Y.,Wharton, S.A.,Lin, Y.P.,Coombs, P.J.,Martin, S.R.,Matrosovich, M.,Chen, Z.,Stevens, D.J.,Hien, V.M.,Thanh, T.T.,Nhu, L.N.T.,Nguyet, L.A.,Ha, D.Q.,van Doorn, H.R.,Hien, T.T.,Conradt, H.S.,Kiso, M.,Gamblin, S.J.,Chai, W.,Skehel, J.J.,Hay, A.J.,Farrar, J.,De Jong, M.D.,Feizi, T.
Changes in the Hemagglutinin of H5N1 Viruses During Human Infection - Influence on Receptor Binding.
Virology, 447:326-, 2013

PubMed Abstract: As avian influenza A(H5N1) viruses continue to circulate in Asia and Africa, global concerns of an imminent pandemic persist. Recent experimental studies suggest that efficient transmission between humans of current H5N1 viruses only requires a few genetic changes. An essential step is alteration of the virus hemagglutinin from preferential binding to avian receptors for the recognition of human receptors present in the upper airway. We have identified receptor-binding changes which emerged during H5N1 infection of humans, due to single amino acid substitutions, Ala134Val and Ile151Phe, in the hemagglutinin. Detailed biological, receptor-binding, and structural analyses revealed reduced binding of the mutated viruses to avian-like receptors, but without commensurate increased binding to the human-like receptors investigated, possibly reflecting a receptor-binding phenotype intermediate in adaptation to more human-like characteristics. These observations emphasize that evolution in nature of avian H5N1 viruses to efficient binding of human receptors is a complex multistep process.

PubMed: 24050651
DOI: 10.1016/J.VIROL.2013.08.010

Experimental method

X-RAY DIFFRACTION (2.5 Å)