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首页> 外文期刊>PLoS Pathogens >Association of host protein VARICOSE with HCPro within a multiprotein complex is crucial for RNA silencing suppression, translation, encapsidation and systemic spread of potato virus A infection
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Association of host protein VARICOSE with HCPro within a multiprotein complex is crucial for RNA silencing suppression, translation, encapsidation and systemic spread of potato virus A infection

机译：Host蛋白静脉曲张在多粒蛋白复合物中与HCPRO的缔解者对RNA沉默抑制，翻译，封装和系统蔓延感染的关键

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In this study, we investigated the significance of a conserved five-amino acid motif ‘AELPR’ in the C-terminal region of helper component–proteinase (HCPro) for potato virus A (PVA; genus Potyvirus ) infection. This motif is a putative interaction site for WD40 domain-containing proteins, including VARICOSE (VCS). We abolished the interaction site in HCPro by replacing glutamic acid (E) and arginine (R) with alanines (A) to generate HCPro WD . These mutations partially eliminated HCPro-VCS co-localization in cells. We have earlier described potyvirus-induced RNA granules (PGs) in which HCPro and VCS co-localize and proposed that they have a role in RNA silencing suppression. We now demonstrate that the ability of HCPro WD to induce PGs, introduce VCS into PGs, and suppress RNA silencing was impaired. Accordingly, PVA carrying HCPro WD (PVA WD ) infected Nicotiana benthamiana less efficiently than wild-type PVA (PVA WT ) and HCPro WD complemented the lack of HCPro in PVA gene expression only partially. HCPro was purified from PVA-infected leaves as part of high molecular weight (HMW) ribonucleoprotein (RNP) complexes. These complexes were more stable when associated with wild-type HCPro than with HCPro WD . Moreover, VCS and two viral components of the HMW-complexes, viral protein genome-linked and cylindrical inclusion protein were specifically decreased in HCPro WD -containing HMW-complexes. A VPg-mediated boost in translation of replication-deficient PVA (PVA ΔGDD ) was observed only if viral RNA expressed wild-type HCPro. The role of VCS-VPg-HCPro coordination in PVA translation was further supported by results from VCS silencing and overexpression experiments and by significantly elevated PVA-derived Renilla luciferase vs PVA RNA ratio upon VPg-VCS co-expression. Finally, we found that PVA WD was unable to form virus particles or to spread systemically in the infected plant. We highlight the role of HCPro-VCS containing multiprotein assemblies associated with PVA RNA in protecting it from degradation, ensuring efficient translation, formation of stable virions and establishment of systemic infection.
机译：在这项研究中，我们研究了Parate蛋白蛋白酶（PVA; Potvirus）感染的助手组分 - 蛋白酶（HCPRO）的C末端区域中保守的五氨基酸基序'AEELPR'的重要性。该基序是含WD40域蛋白质的推定相互作用位点，包括静脉曲张（VCs）。通过用丙氨酸（A）代替谷氨酸（E）和精氨酸（R）来消除HcPro中的相互作用位点以产生HCPRO WD。这些突变部分消除了细胞中的HCPRO-VCS共定位。我们早先描述了potyvirus诱导的RNA颗粒（PGS），其中HCPRO和VCs共定，并提出它们在RNA沉默抑制中具有作用。我们现在证明HCPRO WD诱导PGS的能力将VCS引入PGS，并抑制RNA沉默被损害。因此，携带HCPRO WD（PVA WD）的PVA比野生型PVA（PVA WT）较少地感染尼古特氏植物，并且HCPRO WD仅部分地部分地互补PVA基因表达中的HCPRO。从PVA感染的叶片纯化HCPRO，作为高分子量（HMW）核糖蛋白（RNP）配合物的一部分。当与野生型HCPRO相关时，这些配合物比与HCPRO WD相关联更稳定。此外，在HMW-复合物的VCS和两种病毒组分，病毒蛋白基因组连接和圆柱夹杂物蛋白在HCPRO WD - 悬浮的HMW络合物中特别降低。仅当病毒RNA表达野生型HCPRO时，才观察到复制缺陷PVA（PVAΔGDD）的翻译中的VPG介导的增压。 VCS-VPG-HCPRO协调在PVA翻译中的作用进一步支持VCS沉默和过表达实验的结果，并通过显着升高的PVA衍生的尼郎荧光素酶对VPG-VCS共表达的PVA RNA比率。最后，我们发现PVA WD无法形成病毒颗粒或在受感染的植物中全身蔓延。我们突出了HCPRO-VCS含有与PVA RNA相关的多点蛋白组件的作用，保护其免于降解，确保有效的翻译，形成稳定的病毒群和系统性感染。

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