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• W2000728863 abstract "Plant viruses depend on the host translational machinery to establish their infectious cycle. In a recent Nature publication, Zorzatto et al., 2015Zorzatto C. Machado J.P.B. Lopes K.V.G. Nascimento K.J.T. Pereira W.A. Brustolini O.J.B. Reis P.A. Calil I.P. Deguchi M. Sachetto-Martins G. et al.Nature. 2015; (Published online February 23, 2015)https://doi.org/10.1038/nature14171Crossref PubMed Scopus (134) Google Scholar highlight the suppression of the protein synthesis process as an antiviral defense mechanism in plants. Plant viruses depend on the host translational machinery to establish their infectious cycle. In a recent Nature publication, Zorzatto et al., 2015Zorzatto C. Machado J.P.B. Lopes K.V.G. Nascimento K.J.T. Pereira W.A. Brustolini O.J.B. Reis P.A. Calil I.P. Deguchi M. Sachetto-Martins G. et al.Nature. 2015; (Published online February 23, 2015)https://doi.org/10.1038/nature14171Crossref PubMed Scopus (134) Google Scholar highlight the suppression of the protein synthesis process as an antiviral defense mechanism in plants. As plants do not possess specialized defense cells, immunity in plants relies on the capacity of every cell to detect pathogens and activate defense responses. One of the major plant defense mechanisms against pathogenic viruses is based on RNA interference, in which the host cellular machinery targets virus-derived nucleic acids (Nicaise, 2014Nicaise V. Front. Plant Sci. 2014; 5: 660Crossref PubMed Scopus (200) Google Scholar). In addition, Resistance (R) proteins recognize virus avirulence factors and trigger an array of physiological and biochemical defense processes broadly targeting pathogens (Nicaise, 2014Nicaise V. Front. Plant Sci. 2014; 5: 660Crossref PubMed Scopus (200) Google Scholar). Plant-virus compatibility is defined by the ability of viral agents to recruit cellular proteins required for the completion of their infectious cycle. Indeed, as acellular parasites with a restricted genome that encodes only a few proteins, plant viruses depend almost exclusively on host metabolism for multiplication and invasion. Thus, viruses face the challenge of hijacking the host machinery at each step of their infection cycle, while they also have to cope with the arsenal of plant defense mechanisms. Geminiviruses, which include begomoviruses, constitute one of the largest and most successful families of plant viruses. Their single-stranded DNA circular genomes are packed in twinned isometric particles and are converted to double-strand forms in the nucleus of infected cells. In the last decades, various strategies employed by viruses to suppress plant immune mechanisms have been uncovered through the identification of host functions subverted by viral proteins. Likewise, the identification of cellular interactors of geminivirus nuclear shuttle proteins (NSPs) has recently revealed the existence of a novel defense pathway against viruses in plants. Initially named after their characterization as virulence targets of begomoviruses through their interaction with viral NSPs, NIKs (NSP-interacting kinases) are plasma membrane-localized leucine-rich repeat (LRR) receptor-like kinases (RLKs) carrying a functional serine/threonine kinase domain (Fontes et al., 2004Fontes E.P.B. Santos A.A. Luz D.F. Waclawovsky A.J. Chory J. Genes Dev. 2004; 18: 2545-2556Crossref PubMed Scopus (151) Google Scholar). In Arabidopsis, they are encoded by a small multigenic family belonging to the LRR-RLKII subfamily and comprise the genes NIK1 (At5g16000), NIK2 (At3g25560), and NIK3 (At1g60800). The function of NIK proteins in countering virus infection was first revealed by the enhanced susceptibility of nik-deficient plants to begomovirus infection (Fontes et al., 2004Fontes E.P.B. Santos A.A. Luz D.F. Waclawovsky A.J. Chory J. Genes Dev. 2004; 18: 2545-2556Crossref PubMed Scopus (151) Google Scholar). NSP-NIK interaction during plant infection was shown to increase virus pathogenicity (Fontes et al., 2004Fontes E.P.B. Santos A.A. Luz D.F. Waclawovsky A.J. Chory J. Genes Dev. 2004; 18: 2545-2556Crossref PubMed Scopus (151) Google Scholar). Over the years, new insights into the components and regulatory mechanisms of the NIK-mediated pathway have emerged, especially through the characterization of NIK1 signaling. Thus, during geminivirus infection, NIK1 oligomerizes and transphosphorylates the kinase domain on a key threonine residue at the position 474 (T474), leading to NIK1 kinase activation (Carvalho et al., 2008Carvalho C.M. Santos A.A. Pires S.R. Rocha C.S. Saraiva D.I. Machado J.P.B. Mattos E.C. Fietto L.G. Fontes E.P.B. PLoS Pathog. 2008; 4: e1000247Crossref PubMed Scopus (90) Google Scholar, Santos et al., 2009Santos A.A. Carvalho C.M. Florentino L.H. Ramos H.J.O. Fontes E.P.B. PLoS ONE. 2009; 4: e5781Crossref PubMed Scopus (36) Google Scholar). Once activated, NIK1 phosphorylates the cytoplasmic ribosomal protein L10 (RPL10), which subsequently relocates to the nucleus to mount a defense response that negatively impacts virus infection (Carvalho et al., 2008Carvalho C.M. Santos A.A. Pires S.R. Rocha C.S. Saraiva D.I. Machado J.P.B. Mattos E.C. Fietto L.G. Fontes E.P.B. PLoS Pathog. 2008; 4: e1000247Crossref PubMed Scopus (90) Google Scholar). The binding of virus-encoded NSPs on the NIK1 kinase domain prevents T474 phosphorylation, interrupting NIK1 downstream signaling by trapping RPL10 within the cytoplasm and ultimately enabling virus proliferation and spread (Santos et al., 2009Santos A.A. Carvalho C.M. Florentino L.H. Ramos H.J.O. Fontes E.P.B. PLoS ONE. 2009; 4: e5781Crossref PubMed Scopus (36) Google Scholar; Figure 1). To gain further mechanistic insights into the role of NIK1 in antiviral immunity, Zorzatto et al., 2015Zorzatto C. Machado J.P.B. Lopes K.V.G. Nascimento K.J.T. Pereira W.A. Brustolini O.J.B. Reis P.A. Calil I.P. Deguchi M. Sachetto-Martins G. et al.Nature. 2015; (Published online February 23, 2015)https://doi.org/10.1038/nature14171Crossref PubMed Scopus (134) Google Scholar used Arabidopsis transgenic lines expressing the NIK1 phosphomimetic gain-of-function mutant T474D and investigated immediate downstream events in the pathway. Whereas the expression of typical defense marker genes associated to gene silencing, salicylic acid, or PAMP-triggered immunity (PTI) pathways was not modulated by NIK1 activation, transcriptomic analyses on T474D plants revealed a downregulation of genes involved in protein translation, suggesting that NIK1 negatively regulates the host translational machinery. This hypothesis was confirmed by a decrease in global in vivo protein synthesis upon NIK1 activation, correlating with a reduction of both polysome and monosome fractions. Polysome loading of viral mRNAs in the T474D-infected leaves seems to be severely reduced, suggesting that the translation of viral transcripts is strongly impaired by NIK1-mediated signaling. To directly connect NIK1 signaling pathway with the downregulation of translational-machinery-related genes, the authors searched for RPL10 nuclear partners and identified a MYB-domain-containing transcription factor named LIMYB. The interaction between LIMYB and RPL10 results in the formation of a transcriptional repressor that specifically suppresses the expression of ribosomal protein (RP) genes through the binding of LIMYB on RP gene promoters, consequently downregulating host global translation and limiting virus infection. Altogether, these results demonstrate that the NIK1-mediated pathway controls protein synthesis in cells infected by begomoviruses, providing a new paradigm for antiviral defenses in plants. Data presented in this work are significant in two respects. First, what emerges is a stepwise model of NIK1-mediated defense (Figure 1) in which NIK1 kinase activity and NSP counteraction together illustrate the arm race between viruses and their hosts. The NSP-NIK interaction is conserved for geminivirus NSPs and NIK homologs from different hosts (Santos et al., 2010Santos A.A. Lopes K.V.G. Apfata J.A.C. Fontes E.P.B. J. Exp. Bot. 2010; 61: 3839-3845Crossref PubMed Scopus (59) Google Scholar, Brustolini et al., 2015Brustolini O.J.B. Machado J.P.B. Condori-Apfata J.A. Coco D. Deguchi M. Loriato V.A. Pereira W.A. Alfenas-Zerbini P. Zerbini F.M. Inoue-Nagata A.K. et al.Plant Biotechnol. J. 2015; (Published online February 16, 2015)https://doi.org/10.1111/pbi.12349Crossref PubMed Scopus (33) Google Scholar), suggesting that NIK-mediated antiviral immunity may represent a general defense mechanism successfully overcome by plant viruses. Hence, NSP-NIK interaction could constitute a molecular target for the development of a broad spectrum resistance strategy in the future (Brustolini et al., 2015Brustolini O.J.B. Machado J.P.B. Condori-Apfata J.A. Coco D. Deguchi M. Loriato V.A. Pereira W.A. Alfenas-Zerbini P. Zerbini F.M. Inoue-Nagata A.K. et al.Plant Biotechnol. J. 2015; (Published online February 16, 2015)https://doi.org/10.1111/pbi.12349Crossref PubMed Scopus (33) Google Scholar). Second, Zorzatto and colleagues unraveled the signaling cascade associated with an antiviral defense-related plant RLK. Over the past 15 years, plant immunity against non-viral pathogens has been strongly associated with RLKs, which either function as pattern recognition receptors (PRRs) that perceive pathogen-associated molecular patterns (PAMPs) or regulate signaling downstream of PRRs. Among them, the LRR-RLKII subfamily member BAK1 (BRI1-associated kinase 1) plays a key role in PTI in many different pathosystems including viruses (Kim et al., 2013Kim B.H. Kim S.Y. Nam K.H. Mol. Cells. 2013; 35: 7-16Crossref PubMed Scopus (37) Google Scholar, Kørner et al., 2013Kørner C.J. Klauser D. Niehl A. Domínguez-Ferreras A. Chinchilla D. Boller T. Heinlein M. Hann D.R. Mol. Plant Microbe Interact. 2013; 26: 1271-1280Crossref PubMed Scopus (105) Google Scholar). NIK proteins, which belong to the same subfamily, are now proved by the authors to be involved in a plant antiviral mechanism, expanding the conceptual relevance of the LRR-RLKII subfamily in plant-pathogen interactions. Irrespective of whether virus genomes are RNA or DNA, and regardless of the host organism, the synthesis of viral proteins is absolutely crucial for the infection success, and numerous translational factors are hijacked by both animal and plant viruses in favor of their multiplication (Walsh and Mohr, 2011Walsh D. Mohr I. Nat. Rev. Microbiol. 2011; 9: 860-875Crossref PubMed Scopus (316) Google Scholar, Nicaise, 2014Nicaise V. Front. Plant Sci. 2014; 5: 660Crossref PubMed Scopus (200) Google Scholar). Furthermore, viruses not only ensure that viral proteins will be produced, but also adopt various strategies to subvert host cellular functions. This includes the shutoff of the host cap-dependent protein synthesis, as reported for many animal viruses (Walsh and Mohr, 2011Walsh D. Mohr I. Nat. Rev. Microbiol. 2011; 9: 860-875Crossref PubMed Scopus (316) Google Scholar). In this context, Zorzatto and colleagues report the suppression of protein translation as a plant antiviral immunity pathway, which is successfully targeted by geminiviruses to enable host colonization. Similar to other LRR-RLKII subfamily members that act as co-receptors for stimulus-dependent ligand-binding receptors, NIK1 might regulate cellular pathways through its interaction with as yet unidentified RLKs. The fact that the modulation of NIK expression leads to classical phenotypes that antagonize those associated to the RLK BRI1 (Brassinosteroid-insensitive 1), a steroid phytohormone receptor involved in plant development, could suggest that NIK1 is involved in the BR11-dependent pathway (Santos et al., 2010Santos A.A. Lopes K.V.G. Apfata J.A.C. Fontes E.P.B. J. Exp. Bot. 2010; 61: 3839-3845Crossref PubMed Scopus (59) Google Scholar). The molecular basis for such cross-talk is yet to be demonstrated. The nature of the molecular signal triggering NIK1 activation during plant infection is currently unknown. Whether it corresponds to a stress-related molecule released by infected cells or to a virus-derived molecule has yet to be revealed. Even if T474D-associated transcriptomic analyses did not reveal any classical PTI markers (Zorzatto et al., 2015Zorzatto C. Machado J.P.B. Lopes K.V.G. Nascimento K.J.T. Pereira W.A. Brustolini O.J.B. Reis P.A. Calil I.P. Deguchi M. Sachetto-Martins G. et al.Nature. 2015; (Published online February 23, 2015)https://doi.org/10.1038/nature14171Crossref PubMed Scopus (134) Google Scholar), given NIK1 structure and function it is reasonable to consider that NIK1 might be activated by a plant PRR specialized in virus PAMP perception. Moreover, the fact that BAK1 has been recently involved in plant-virus interactions (Kørner et al., 2013Kørner C.J. Klauser D. Niehl A. Domínguez-Ferreras A. Chinchilla D. Boller T. Heinlein M. Hann D.R. Mol. Plant Microbe Interact. 2013; 26: 1271-1280Crossref PubMed Scopus (105) Google Scholar) raises the question of possible connections between BAK1 and NIK1 pathways during virus infection. Answers to all these questions should provide important insights into plant antiviral immunity and will be of particular interest. V.N. is funded by the European Framework Programme 7 through a Marie-Curie Intra-European Fellowship (grant number 327341)." @default.
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• W2000728863 title "Lost in Translation: An Antiviral Plant Defense Mechanism Revealed" @default.
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