Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts

Maroniche, Guillermo Andrés; Mongelli, Vanesa; Peralta, Andrea; Distéfano, Ana Julia; Llauger, Gabriela; Taboga, Oscar; Hopp, H. Esteban; Vas, Mariana del

doi:10.1016/j.virusres.2010.06.010

Cited by 26 publications

(56 citation statements)

References 41 publications

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“…3), confirming the hypothesis that the viroplasm is the site for the replication and assembly of fijiviruses. Our results extend the limited information from previous electron microscopic studies that showed that P9-1 of two other fijiviruses (RBSDV and MRCV) exclusively localized in the matrix of viroplasms in virus-infected cells (9,12,19). With the evidence indicating that P9-1 alone was necessary for the formation of viroplasm-like structures in nonhost cells (Fig.…”

Section: Discussionsupporting

confidence: 89%

“…4B). It has been shown that the carboxy-terminal portion of P9-1 of two other fijiviruses, i.e., RBSDV and Mal de Río Cuarto virus (MRCV), contained important domains required for the formation of viroplasm-like structures (1,19). To confirm a similar functional role for the carboxyterminal portion of SRBSDV in the formation of viroplasm-like structures, we generated a P9-1 mutant in which the C-terminal 20 residues were deleted (P9-1⌬C) and found that this mutant was diffusely distributed in the cytoplasm (Fig.…”

Section: Srbsdv P9-1 Was Sufficient To Induce Formation Of Viroplasm-mentioning

confidence: 99%

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Development of an Insect Vector Cell Culture and RNA Interference System To Investigate the Functional Role of Fijivirus Replication Protein

Jia

Chen

Zheng

et al. 2012

J Virol

109

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Section: Discussionsupporting

confidence: 89%

Section: Srbsdv P9-1 Was Sufficient To Induce Formation Of Viroplasm-mentioning

confidence: 99%

Development of an Insect Vector Cell Culture and RNA Interference System To Investigate the Functional Role of Fijivirus Replication Protein

Jia

Chen

Zheng

et al. 2012

J Virol

109

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“…The P9-1 protein of Mal de Río Cuarto virus (MRCV), a counterpart of the P9-1 protein of RBSDV, has also been shown to self-associate, giving rise to different high-molecular-weight oligomers when expressed in bacteria (37). The RBSDV P9-1 protein shares 63% amino acid identity with the P9-1 protein of MRCV, which is in the same genus (Fijivirus) and family (Reoviridae) as RBSDV.…”

Section: Discussionmentioning

confidence: 99%

“…The RBSDV P9-1 protein shares 63% amino acid identity with the P9-1 protein of MRCV, which is in the same genus (Fijivirus) and family (Reoviridae) as RBSDV. The amino acid similarity between the two viruses suggests that their P9-1 proteins may have similar biochemical properties, such as nonspecific RNA binding activity (37).…”

Section: Discussionmentioning

confidence: 99%

Viroplasm Protein P9-1 of Rice Black-Streaked Dwarf Virus Preferentially Binds to Single-Stranded RNA in Its Octamer Form, and the Central Interior Structure Formed by This Octamer Constitutes the Major RNA Binding Site

Wang

et al. 2013

J Virol

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f The P9-1 protein of Rice black-streaked dwarf virus (RBSDV) is an essential part of the viroplasm. However, little is known about its nature or biological function in the viroplasm. In this study, the structure and function of P9-1 were analyzed for in vitro binding to nucleic acids. We found that the P9-1 protein preferentially bound to single-stranded versus double-stranded nucleic acids; however, the protein displayed no preference for RBSDV versus non-RBSDV single-stranded ssRNA (ssRNA). A gel mobility shift assay revealed that the RNA gradually shifted as increasing amounts of P9-1 were added, suggesting that multiple subunits of P9-1 bind to ssRNA. By using discontinuous blue native gel and chromatography analysis, we found that the P9-1 protein was capable of forming dimers, tetramers, and octamers. Strikingly, we demonstrated that P9-1 preferentially bound to ssRNA in the octamer, rather than the dimer, form. Deletion of the C-terminal arm resulted in P9-1 no longer forming octamers; consequently, the deletion mutant protein bound to ssRNA with significantly lower affinity and with fewer copies bound per ssRNA. Alanine substitution analysis revealed that electropositive amino acids among residues 25 to 44 are important for RNA binding and map to the central interior structure that was formed only by P9-1 octamers. Collectively, our findings provide novel insights into the structure and function of RBSDV viroplasm protein P9-1 binding to RNA.

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“…For application in GCRV protein-protein interaction identification, GCRV873 (GCRV genotype I) NS80 is verified to interact with proteins NS38, VP4, and VP6 as well as itself, whereas no interactions involving the four protein pairs NS38-VP4, NS38-VP6, VP4-VP4, and VP4-VP6 are observed [6]. Strong selfinteraction is evidenced in Rice black-streaked dwarf virus (RBSDV) P10 protein, Mal de Río Cuarto virus (MRCV) P9-1 protein, and avian orthoreovirus (ARV) lNS protein through Y2H assays [5,20,22]. To elucidate the basic role of VP6 protein in GCRV-AH528 (GCRV genotype II) replication and particle assembly, Y2H system was used to identify VP6 self-interaction.…”

Section: Discussionmentioning

confidence: 98%

Structure and function of S9 segment of grass carp reovirus Anhui strain

Jiang

et al. 2017

VirusDis.

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A highly virulent grass carp reovirus (GCRV) strain, named GCRV-AH528, was recently purified from a diseased grass carp with hemorrhage disease in Anhui, China. GCRV-AH528 S9 segment was 1320 nucleotides in length and encoded a 418 amino acid VP6 protein. BLAST search showed that the VP6 protein owned a conserved domain belonging to the reoviral r2 family. Phylogenetic analysis of VP6 presented that GCRV-AH528 belonged to GCRV genotype II, which was more closely related to Orthoreovirus than GCRV genotype I and genotype III. Further analysis revealed that GCRV-AH528 S9 and mammalian orthoreovirus S8 might have evolved from a common ancestral precursor and have identical mechanism in virus assembly. The expression level of vp6 gene was detected by quantitative real-time PCR (qRT-PCR). Over time, the expression level of vp6 gradually increased in Ctenopharyngodon idellus kidney cells. However, the level of vp6 expression in blood sharply increased at 4-6 days, and then decreased to a low level after GCRV-AH528 challenge (P \ 0.05). The vp6 gene was detected in all tissues examined, whereas at relatively higher levels in blood, kidney, and liver (P \ 0.05). The yeast two-hybrid (Y2H) system was used to identify VP6 self-interaction, while no interaction was detected in VP6-VP6. This study not only revealed the S9 segment structure and expression pattern but also analyzed the VP6 mechanism by yeast hybridization method. The present study provides valuable informations for further experimental design and investigation of VP6 functions.

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Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts

Cited by 26 publications

References 41 publications

Development of an Insect Vector Cell Culture and RNA Interference System To Investigate the Functional Role of Fijivirus Replication Protein

Development of an Insect Vector Cell Culture and RNA Interference System To Investigate the Functional Role of Fijivirus Replication Protein

Viroplasm Protein P9-1 of Rice Black-Streaked Dwarf Virus Preferentially Binds to Single-Stranded RNA in Its Octamer Form, and the Central Interior Structure Formed by This Octamer Constitutes the Major RNA Binding Site

Structure and function of S9 segment of grass carp reovirus Anhui strain

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