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高致病性猪繁殖与呼吸综合征病毒核衣壳蛋白的生物物理特性分析。

Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain.

机构信息

Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 6JP, UK.

出版信息

Biochem Biophys Res Commun. 2012 Mar 9;419(2):137-41. doi: 10.1016/j.bbrc.2011.11.126. Epub 2012 Jan 28.

DOI:10.1016/j.bbrc.2011.11.126
PMID:22306009
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7092862/
Abstract

The arterivirus nucleocapsid (N) protein is a multifunctional protein that binds viral RNA for encapsidation and has potential roles in host cell processes. This study characterised the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). The association with viral RNA was mapped to defined motifs on the N protein. The results indicated that disulphide bridge formation played a key role in RNA binding, offering an explanation why infectious virus cannot be rescued if cysteine residues are mutated, and that multiple sites may promote RNA binding.

摘要

动脉炎病毒核衣壳(N)蛋白是一种多功能蛋白,可结合病毒 RNA 进行包裹,并在宿主细胞过程中具有潜在作用。本研究对来自北美高致病性猪繁殖与呼吸综合征病毒(PRRSV)的 N 蛋白进行了特征描述。N 蛋白与病毒 RNA 的结合被定位到 N 蛋白上的特定基序。结果表明,二硫键的形成在 RNA 结合中起着关键作用,这解释了为什么如果半胱氨酸残基发生突变,就无法拯救感染性病毒,并且多个位点可能促进 RNA 结合。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/5b2917a6f333/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/6d9e064f5dba/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/ec6e65e31798/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/e995c6469e48/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/5b2917a6f333/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/6d9e064f5dba/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/ec6e65e31798/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/e995c6469e48/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9112/7092862/5b2917a6f333/gr4.jpg

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本文引用的文献

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The structural biology of PRRSV.猪繁殖与呼吸综合征病毒的结构生物学。
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2
Modulation of host cell responses and evasion strategies for porcine reproductive and respiratory syndrome virus.猪繁殖与呼吸综合征病毒宿主细胞反应的调节和逃逸策略。
Virus Res. 2010 Dec;154(1-2):48-60. doi: 10.1016/j.virusres.2010.07.019. Epub 2010 Jul 23.
3
Cryo-electron tomography of porcine reproductive and respiratory syndrome virus: organization of the nucleocapsid.
来自高致病性猪繁殖与呼吸综合征病毒分离株的核衣壳蛋白细胞蛋白质组解析确定PARP-1为一种细胞靶点,其相互作用对病毒生物学至关重要。
Vet Microbiol. 2015 Mar 23;176(1-2):109-19. doi: 10.1016/j.vetmic.2014.11.023. Epub 2014 Dec 30.
4
Cecropin P1 inhibits porcine reproductive and respiratory syndrome virus by blocking attachment.天蚕素P1通过阻断病毒附着来抑制猪繁殖与呼吸综合征病毒。
BMC Microbiol. 2014 Nov 18;14:273. doi: 10.1186/s12866-014-0273-8.
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RNA interference targeting nucleocapsid protein inhibits porcine reproductive and respiratory syndrome virus replication in Marc-145 cells.靶向核衣壳蛋白的RNA干扰抑制猪繁殖与呼吸综合征病毒在Marc-145细胞中的复制。
J Microbiol. 2014 Apr;52(4):333-9. doi: 10.1007/s12275-014-3419-3. Epub 2014 Mar 29.
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