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4WA3

The crystal structure of neuraminidase from a H3N8 influenza virus isolated from New England harbor seals

Summary for 4WA3
Entry DOI10.2210/pdb4wa3/pdb
Related4WA1 4WA2 4WA4 4WA5
DescriptorNeuraminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose, ... (6 entities in total)
Functional Keywordsneuraminidase, influenza virus, seal, viral protein
Biological sourceInfluenza A virus (A/harbor seal/Massachusetts/1/2011(H3N8))
Cellular locationHost apical cell membrane ; Single-pass type II membrane protein : I6NW33
Total number of polymer chains1
Total formula weight43420.47
Authors
Yang, H.,Villanueva, J.M.,Gubareva, L.V.,Stevens, J. (deposition date: 2014-08-28, release date: 2015-01-14, Last modification date: 2023-09-27)
Primary citationYang, H.,Nguyen, H.T.,Carney, P.J.,Guo, Z.,Chang, J.C.,Jones, J.,Davis, C.T.,Villanueva, J.M.,Gubareva, L.V.,Stevens, J.
Structural and Functional Analysis of Surface Proteins from an A(H3N8) Influenza Virus Isolated from New England Harbor Seals.
J.Virol., 89:2801-2812, 2015
Cited by
PubMed Abstract: In late 2011, an A(H3N8) influenza virus infection resulted in the deaths of 162 New England harbor seals. Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference (S. J. Anthony, J. A. St Leger, K. Pugliares, H. S. Ip, J. M. Chan, Z. W. Carpenter, I. Navarrete-Macias, M. Sanchez-Leon, J. T. Saliki, J. Pedersen, W. Karesh, P. Daszak, R. Rabadan, T. Rowles, W. I. Lipkin, MBio 3:e00166-00112, 2012, http://dx.doi.org/10.1128/mBio.00166-12). Here, we present a detailed structural and biochemical analysis of the surface antigens of the virus. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase indicate a true avian receptor binding preference. Although the detection of this virus in new species highlights an increased potential for cross-species transmission, our results indicate that the A(H3N8) virus currently poses a low risk to humans.
PubMed: 25540377
DOI: 10.1128/JVI.02723-14
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.801 Å)
Structure validation

226707

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