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5H5N

The crystal structure of the NS1 (H17N10) RNA-binding domain

Summary for 5H5N
Entry DOI10.2210/pdb5h5n/pdb
DescriptorNon-structural protein 1 (2 entities in total)
Functional Keywordsinfluenza virus, rna-binding domain, rna binding protein
Biological sourceInfluenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))
Cellular locationHost cytoplasm : H6QM99
Total number of polymer chains2
Total formula weight17137.71
Authors
Zhao, X.,Qi, J.,Xiao, H.,Gao, G.F. (deposition date: 2016-11-08, release date: 2016-11-23, Last modification date: 2023-11-08)
Primary citationZhao, X.,Tefsen, B.,Li, Y.,Qi, J.,Lu, G.,Shi, Y.,Yan, J.,Xiao, H.,Gao, G.F.
The NS1 gene from bat-derived influenza-like virus H17N10 can be rescued in influenza A PR8 backbone
J.Gen.Virol., 97:1797-1806, 2016
Cited by
PubMed Abstract: Influenza A viruses have the potential to cause pandemics due to the introduction of novel subtypes against which human hosts have little or no preexisting immunity. Such viruses may result from reassortment between human and animal influenza viruses. Recently, new influenza-like viruses were identified in bats, raising the concern for a new reservoir of potentially harmful influenza viruses that could form reassortants with categorized human influenza A viruses. However, until now, it has not been possible to generate a recombinant reassortant virus containing a single functional gene or domain from H17N10 that could propagate. Here, we demonstrate that a recombinant A/Puerto Rico/8/1934 (H1N1) virus with NS1 gene from H17N10 influenza-like virus can be successfully rescued. We used luciferase reporter assays and quantitative reverse transcriptase PCR to show that the NS1 protein from H17N10 inhibited Sendai-virus (SeV)-induced activation of IFN-β expression with an efficiency similar to NS1 from an H5N1 strain. Moreover, the crystal structure of the NS1 (H17N10) RNA-binding domain is also similar to that of other NS1s. These results demonstrate that H17N10 influenza-like virus indeed contains functional genes that are compatible with categorized influenza A viruses. Although the chance of this particular event occurring in nature seems negligible, further research is needed to address the possibility of the natural formation of reassortants.
PubMed: 27217257
DOI: 10.1099/jgv.0.000509
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

239149

數據於2025-07-23公開中

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