5H5N

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

5H5N の概要

• エントリーDOI: 10.2210/pdb5h5n/pdb
• 分子名称: Non-structural protein 1 (2 entities in total)
• 機能のキーワード: influenza virus, rna-binding domain, rna binding protein
• 由来する生物種: Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))
• 細胞内の位置: Host cytoplasm : H6QM99
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17137.71

構造登録者

Zhao, X.,Qi, J.,Xiao, H.,Gao, G.F. (登録日: 2016-11-08, 公開日: 2016-11-23, 最終更新日: 2023-11-08)

主引用文献

Zhao, 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

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

実験手法

X-RAY DIFFRACTION (2 Å)