Pérez-Cañamás Miryam, Taliansky Michael, Hernández Carmen
Instituto de Biología Molecular y Celular de Plantas (Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia), Ciudad Politécnica de la Innovación, Calle Ingeniero Fausto Elio, Ed. 8E. Camino de Vera s/n, 46022 Valencia, Spain.
The James Hutton Institute, Invergowrie, Dundee DD2 5DA, UK.
Plants (Basel). 2022 Jul 22;11(15):1903. doi: 10.3390/plants11151903.
To establish productive infections, viruses must be able both to subdue the host metabolism for their own benefit and to counteract host defences. This frequently results in the establishment of viral-host protein-protein interactions that may have either proviral or antiviral functions. The study of such interactions is essential for understanding the virus-host interplay. Plant viruses with RNA genomes are typically translated, replicated, and encapsidated in the cytoplasm of infected cells. Despite this, a significant array of their encoded proteins has been reported to enter the nucleus, often showing high accumulation at subnuclear structures such as the nucleolus and/or Cajal bodies. However, the biological significance of such a distribution pattern is frequently unknown. Here, we explored whether the nucleolar/Cajal body localization of protein p37 of (PLPV, genus , family ), might be related to potential interactions with the nucleolar/Cajal body marker proteins, fibrillarin and coilin. The results revealed that p37, which has a dual role as coat protein and as suppressor of RNA silencing, a major antiviral system in plants, is able to associate with these cellular factors. Analysis of (wildtype and/or mutant) PLPV accumulation in plants with up- or downregulated levels of fibrillarin or coilin have suggested that the former might be involved in an as yet unknown antiviral pathway, which may be targeted by p37. The results suggest that the growing number of functions uncovered for fibrillarin can be wider and may prompt future investigations to unveil the plant antiviral responses in which this key nucleolar component may take part.
为了建立有效的感染，病毒必须既能为自身利益而抑制宿主代谢，又能对抗宿主防御。这常常导致病毒与宿主之间形成蛋白质 - 蛋白质相互作用，这些相互作用可能具有促进病毒感染或抗病毒的功能。研究此类相互作用对于理解病毒与宿主的相互作用至关重要。具有RNA基因组的植物病毒通常在受感染细胞的细胞质中进行翻译、复制和衣壳化。尽管如此，据报道它们的大量编码蛋白会进入细胞核，并且常常在核仁及/或卡哈尔体等亚核结构中高度积累。然而，这种分布模式的生物学意义通常尚不明确。在这里，我们探究了李痘病毒属（李痘病毒，属，科）蛋白p37在核仁/卡哈尔体中的定位是否可能与它和核仁/卡哈尔体标记蛋白原纤维蛋白及卷曲螺旋蛋白的潜在相互作用有关。结果表明，兼具外壳蛋白和RNA沉默抑制子（植物中的一种主要抗病毒系统）双重作用的p37能够与这些细胞因子相互作用。对原纤维蛋白或卷曲螺旋蛋白水平上调或下调的植物中（野生型和/或突变型）李痘病毒积累情况的分析表明，前者可能参与了一条尚未明确的抗病毒途径，而p37可能靶向该途径。结果表明，已发现的原纤维蛋白越来越多的功能范围可能更广，这可能促使未来开展研究以揭示这个关键核仁成分可能参与的植物抗病毒反应。
