5HUM
The crystal structure of neuraminidase from A/Sichuan/26221/2014 influenza virus
Summary for 5HUM
| Entry DOI | 10.2210/pdb5hum/pdb |
| Related | 5HUF 5HUG 5HUK 5HUN |
| Descriptor | neuraminidase, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | neuraminidase, influenza virus, h5nx, viral protein |
| Biological source | Influenza A virus (A/chicken/Sichuan/NCJPL1/2014(H5N6)) |
| Total number of polymer chains | 4 |
| Total formula weight | 174785.08 |
| Authors | Yang, H.,Carney, P.J.,Guo, Z.,Chang, J.C.,Stevens, J. (deposition date: 2016-01-27, release date: 2016-04-13, Last modification date: 2020-07-29) |
| Primary citation | Yang, H.,Carney, P.J.,Mishin, V.P.,Guo, Z.,Chang, J.C.,Wentworth, D.E.,Gubareva, L.V.,Stevens, J. Molecular Characterizations of Surface Proteins Hemagglutinin and Neuraminidase from Recent H5Nx Avian Influenza Viruses. J.Virol., 90:5770-5784, 2016 Cited by PubMed Abstract: During 2014, a subclade 2.3.4.4 highly pathogenic avian influenza (HPAI) A(H5N8) virus caused poultry outbreaks around the world. In late 2014/early 2015, the virus was detected in wild birds in Canada and the United States, and these viruses also gave rise to reassortant progeny, composed of viral RNA segments (vRNAs) from both Eurasian and North American lineages. In particular, viruses were found with N1, N2, and N8 neuraminidase vRNAs, and these are collectively referred to as H5Nx viruses. In the United States, more than 48 million domestic birds have been affected. Here we present a detailed structural and biochemical analysis of the surface antigens of H5N1, H5N2, and H5N8 viruses in addition to those of a recent human H5N6 virus. Our results with recombinant hemagglutinin reveal that these viruses have a strict avian receptor binding preference, while recombinantly expressed neuraminidases are sensitive to FDA-approved and investigational antivirals. Although H5Nx viruses currently pose a low risk to humans, it is important to maintain surveillance of these circulating viruses and to continually assess future changes that may increase their pandemic potential. PubMed: 27053557DOI: 10.1128/JVI.00180-16 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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