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Pathogenesis mediated by proviral host factors involved in translation and replication of plant positive-strand RNA viruses 査読

Kiwamu Hyodo, Tetsuro Okuno

CURRENT OPINION IN VIROLOGY 17 11 - 18 2016年4月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：ELSEVIER SCI LTD

Viral pathogenesis comes from complex interactions between viruses and hosts. All the processes of viral infection, including translation of viral factors and replication of viral genomes, define viral pathogenesis; therefore, molecular insights into the mechanisms underlying viral replication strategies unambiguously pave the way for our comprehensive understanding of viral pathogenesis and disease outcome, as well as for developing new antiviral strategies against plant virus disease. Recent studies of plant positive-strand RNA [(+)RNA] viruses have advanced our understanding of co-opted host factors and their roles in viral translation and replication. It is becoming clear that plant (+)RNA viruses harness host factors involved in membrane trafficking and lipid metabolism to establish the viral replication complex (VRC). In this review, we aim to discuss the contribution of co-opted host factors in translation and genome replication of plant (+)RNA viruses mainly focusing on those involved in the biogenesis of the VRC, which may act as a central hub in almost all the processes of viral infection as well as viral pathogenesis.

DOI： 10.1016/j.coviro.2015.11.004

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Phosphatidic Acid Produced by Phospholipase D Promotes RNA Replication of a Plant RNA Virus 査読

Kiwamu Hyodo, Takako Taniguchi, Yuki Manabe, Masanori Kaido, Kazuyuki Mise, Tatsuya Sugawara, Hisaaki Taniguchi, Tetsuro Okuno

PLOS PATHOGENS 11 ( 5 ) e1004909 2015年5月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：PUBLIC LIBRARY SCIENCE

Eukaryotic positive-strand RNA [(+) RNA] viruses are intracellular obligate parasites replicate using the membrane-bound replicase complexes that contain multiple viral and host components. To replicate, (+) RNA viruses exploit host resources and modify host metabolism and membrane organization. Phospholipase D (PLD) is a phosphatidylcholine-and phosphatidylethanolamine-hydrolyzing enzyme that catalyzes the production of phosphatidic acid (PA), a lipid second messenger that modulates diverse intracellular signaling in various organisms. PA is normally present in small amounts (less than 1% of total phospholipids), but rapidly and transiently accumulates in lipid bilayers in response to different environmental cues such as biotic and abiotic stresses in plants. However, the precise functions of PLD and PA remain unknown. Here, we report the roles of PLD and PA in genomic RNA replication of a plant (+) RNA virus, Red clover necrotic mosaic virus (RCNMV). We found that RCNMV RNA replication complexes formed in Nicotiana benthamiana contained PLD alpha and PLD beta. Gene-silencing and pharmacological inhibition approaches showed that PLDs and PLDs-derived PA are required for viral RNA replication. Consistent with this, exogenous application of PA enhanced viral RNA replication in plant cells and plant-derived cell-free extracts. We also found that a viral auxiliary replication protein bound to PA in vitro, and that the amount of PA increased in RCNMV-infected plant leaves. Together, our findings suggest that RCNMV hijacks host PA-producing enzymes to replicate.

DOI： 10.1371/journal.ppat.1004909

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GAPDH-A Recruits a Plant Virus Movement Protein to Cortical Virus Replication Complexes to Facilitate Viral Cell-to-Cell Movement 査読

Masanori Kaido, Kazutomo Abe, Akira Mine, Kiwamu Hyodo, Takako Taniguchi, Hisaaki Taniguchi, Kazuyuki Mise, Tetsuro Okuno

PLOS PATHOGENS 10 ( 11 ) e1004505 2014年11月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：PUBLIC LIBRARY SCIENCE

The formation of virus movement protein (MP)-containing punctate structures on the cortical endoplasmic reticulum is required for efficient intercellular movement of Red clover necrotic mosaic virus (RCNMV), a bipartite positive-strand RNA plant virus. We found that these cortical punctate structures constitute a viral replication complex (VRC) in addition to the previously reported aggregate structures that formed adjacent to the nucleus. We identified host proteins that interacted with RCNMV MP in virus-infected Nicotiana benthamiana leaves using a tandem affinity purification method followed by mass spectrometry. One of these host proteins was glyceraldehyde 3-phosphate dehydrogenase-A (NbGAPDH-A), which is a component of the Calvin-Benson cycle in chloroplasts. Virus-induced gene silencing of NbGAPDH-A reduced RCNMV multiplication in the inoculated leaves, but not in the single cells, thereby suggesting that GAPDH-A plays a positive role in cell-to-cell movement of RCNMV. The fusion protein of NbGAPDH-A and green fluorescent protein localized exclusively to the chloroplasts. In the presence of RCNMV RNA1, however, the protein localized to the cortical VRC as well as the chloroplasts. Bimolecular fluorescence complementation assay and GST pulldown assay confirmed in vivo and in vitro interactions, respectively, between the MP and NbGAPDH-A. Furthermore, gene silencing of NbGAPDH-A inhibited MP localization to the cortical VRC. We discuss the possible roles of NbGAPDH-A in the RCNMV movement process.

DOI： 10.1371/journal.ppat.1004505

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Host and viral RNA-binding proteins involved in membrane targeting, replication and intercellular movement of plant RNA virus genomes 査読

K. Hyodo, M. Kaido, T. Okuno

Frontiers in Plant Science 5 321 2014年7月

Traffic jam on the cellular secretory pathway generated by a replication protein from a plant RNA virus 査読

Kiwamu Hyodo, Masanori Kaido, Tetsuro Okuno

Plant Signaling and Behavior 9 2014年

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Landes Bioscience

Although positive-strand RNA [(+)RNA] viruses have a limited coding capacity, they can replicate efficiently in host cells because of their ability to use host-derived proteins, membranes, lipids, and metabolites, and to rewire cellular trafficking pathways. Previously, we showed that a plant RNA virus, the Red clover necrotic mosaic virus (RCNM V), hijacked Arf1 and Sar1, which are small GTPases that regulate the biogenesis of COPI and COPII vesicles, respectively, for viral RNA replication. These small GTPases are relocated from appropriate subcellular compartments to the viral RNA replication sites by p27 replication protein, which raises the possibility that RCNM V interferes with the cellular secretory pathway. Here, we examined this possibility by using green fluorescent protein-fused rice SCAM P1 and Arabidopsis LRR 84A as secretory pathway marker proteins and showed that p27 inhibited the trafficking of these proteins. RCNM Vmediated inhibition of the host secretion pathway and its possible impact on plant-virus interaction are discussed. © 2014 Landes Bioscience.

DOI： 10.4161/psb.28644

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ADPribosylation factor 1 plays an essential role in the replication of a plant RNA virus 査読

Hyodo K, Mine A, Taniguchi T, Kaido M, Mise K, Taniguchi H, Okuno T

J Virol. 87 ( 1 ) 163 - 176 2013年1月

Differential roles of Hsp70 and Hsp90 in the assembly of the replicase complex of a positive-strand RNA plant virus 査読

Mine A, Hyodo K, Tajima Y, Kusumanegara K, Taniguchi T, Kaido M, Mise K, Taniguchi H, Okuno T

J Virol. 86 ( 22 ) 12091 - 12104 2012年11月

記述言語：英語出版者・発行元：American Society for Microbiology

Assembly of viral replicase complexes of eukaryotic positive-strand RNA viruses is a regulated process: multiple viral and host components must be assembled on intracellular membranes and ordered into quaternary complexes capable of synthesizing viral RNAs. However, the molecular mechanisms underlying this process are poorly understood. In this study, we used a model virus, Red clover necrotic mosaic virus (RCNMV), whose replicase complex can be detected readily as the 480-kDa functional protein complex. We found that host heat shock proteins Hsp70 and Hsp90 are required for RCNMV RNA replication and that they interact with p27, a virus-encoded component of the 480-kDa replicase complex, on the endoplasmic reticulum membrane. Using a cell-free viral translation/replication system in combination with specific inhibitors of Hsp70 and Hsp90, we found that inhibition of p27-Hsp70 interaction inhibits the formation of the 480-kDa complex but instead induces the accumulation of large complexes that are nonfunctional in viral RNA synthesis. In contrast, inhibition of p27-Hsp90 interaction did not induce such large complexes but rendered p27 incapable of binding to a specific viral RNA element, which is a critical step for the assembly of the 480-kDa replicase complex and viral RNA replication. Together, our results suggest that Hsp70 and Hsp90 regulate different steps in the assembly of the RCNMV replicase complex.

DOI： 10.1128/JVI.01659-12

Identification of domains in p27 auxiliary replicase protein essential for its association with the endoplasmic reticulum membranes in Red clover necrotic mosaic virus. 査読

Kusumanegara K, Mine A, Hyodo K, Kaido M, Mise K, Okuno T

Virology 433 ( 1 ) 131 - 141 2012年11月

Identification ofamino acids in auxiliary replicase protein p27 critical for its RNA-bindingactivity and the assembly of the replicase complex in Red clover necrotic mosaic virus 査読

Hyodo K, Mine A, Iwakawa HO, Kaido M, Mise K, Okuno T

Virology 413 ( 2 ) 300 - 309 2011年5月

Template recognition mechanisms by replicase proteins differ between bipartitepositive-strand genomic RNAs of a plant virus 査読

Iwakawa HO, Mine A, Hyodo K, An M, Kaido M, Mise K, Okuno T

J Virol. 85 ( 1 ) 497 - 509 2011年1月

記述言語：英語出版者・発行元：American Society for Microbiology

Recognition of RNA templates by viral replicase proteins is one of the key steps in the replication process of all RNA viruses. However, the mechanisms underlying this phenomenon, including primary RNA elements that are recognized by the viral replicase proteins, are not well understood. Here, we used aptamer pulldown assays with membrane fractionation and protein-RNA coimmunoprecipitation in a cell-free viral translation/replication system to investigate how viral replicase proteins recognize the bipartite genomic RNAs of the Red clover necrotic mosaic virus (RCNMV). RCNMV replicase proteins bound specifically to a Y-shaped RNA element (YRE) located in the 3' untranslated region (UTR) of RNA2, which also interacted with the 480-kDa replicase complexes that contain viral and host proteins. The replicase-YRE interaction recruited RNA2 to the membrane fraction. Conversely, RNA1 fragments failed to interact with the replicase proteins supplied in trans. The results of protein-RNA coimmunoprecipitation assays suggest that RNA1 interacts with the replicase proteins coupled with their translation. Thus, the initial template recognition mechanisms employed by the replicase differ between RCNMV bipartite genomic RNAs and RNA elements are primary determinants of the differential replication mechanism.

DOI： 10.1128/JVI.01754-10

Interactions between p27 and p88 replicase proteins of Red clover necrotic mosaic virus play an essential role in viral RNA replication and suppression of RNA silencing via the 480-kDaviral replicase complex assembly 査読

Mine A, Hyodo K, Takeda A, Kaido M, Mise K, Okuno T

Virology 407 ( 2 ) 213 - 224 2010年11月

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