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TRBP and eIF6 Homologue in Marsupenaeus japonicus Play Crucial Roles in Antiviral Response (TRBP and eIF6 in Antiviral Response)

Plants and invertebrates can suppress viral infection through RNA silencing, mediated by RNA-induced silencing complex (RISC). Trans-activation response RNA-binding protein (TRBP), consisting of three double-stranded RNA-binding domains, is a component of the RISC. In our previous paper, a TRBP homo... Full description

Journal Title: PLoS ONE 2012, Vol.7(1), p.e30057
Main Author: Wang, Shuai
Other Authors: Chen, An-Jing , Shi, Li-Jie , Zhao, Xiao-Fan , Wang, Jin-Xing
Format: Electronic Article Electronic Article
Language: English
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ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0030057
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recordid: plos10.1371/journal.pone.0030057
title: TRBP and eIF6 Homologue in Marsupenaeus japonicus Play Crucial Roles in Antiviral Response (TRBP and eIF6 in Antiviral Response)
format: Article
creator:
  • Wang, Shuai
  • Chen, An-Jing
  • Shi, Li-Jie
  • Zhao, Xiao-Fan
  • Wang, Jin-Xing
subjects:
  • Research Article
  • Biology
  • Medicine
  • Physics
  • Genetics And Genomics
  • Immunology
  • Microbiology
  • Molecular Biology
  • Biophysics
  • Physics
  • Biochemistry
ispartof: PLoS ONE, 2012, Vol.7(1), p.e30057
description: Plants and invertebrates can suppress viral infection through RNA silencing, mediated by RNA-induced silencing complex (RISC). Trans-activation response RNA-binding protein (TRBP), consisting of three double-stranded RNA-binding domains, is a component of the RISC. In our previous paper, a TRBP homologue in Fenneropenaeus chinensis ( Fc -TRBP) was reported to directly bind to eukaryotic initiation factor 6 ( Fc -eIF6). In this study, we further characterized the function of TRBP and the involvement of TRBP and eIF6 in antiviral RNA interference (RNAi) pathway of shrimp. The double-stranded RNA binding domains (dsRBDs) B and C of the TRBP from Marsupenaeus japonicus ( Mj -TRBP) were found to mediate the interaction of TRBP and eIF6. Gel-shift assays revealed that the N-terminal of Mj -TRBP dsRBD strongly binds to double-stranded RNA (dsRNA) and that the homodimer of the TRBP mediated by the C-terminal dsRBD increases the affinity to dsRNA. RNAi against either Mj -TRBP or Mj -eIF6 impairs the dsRNA-induced sequence-specific RNAi pathway and facilitates the proliferation of white spot syndrome virus (WSSV). These results further proved the important roles of TRBP and eIF6 in the antiviral response of shrimp.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0030057
fulltext: fulltext
issn:
  • 1932-6203
  • 19326203
url: Link


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titleTRBP and eIF6 Homologue in Marsupenaeus japonicus Play Crucial Roles in Antiviral Response (TRBP and eIF6 in Antiviral Response)
creatorWang, Shuai ; Chen, An-Jing ; Shi, Li-Jie ; Zhao, Xiao-Fan ; Wang, Jin-Xing
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descriptionPlants and invertebrates can suppress viral infection through RNA silencing, mediated by RNA-induced silencing complex (RISC). Trans-activation response RNA-binding protein (TRBP), consisting of three double-stranded RNA-binding domains, is a component of the RISC. In our previous paper, a TRBP homologue in Fenneropenaeus chinensis ( Fc -TRBP) was reported to directly bind to eukaryotic initiation factor 6 ( Fc -eIF6). In this study, we further characterized the function of TRBP and the involvement of TRBP and eIF6 in antiviral RNA interference (RNAi) pathway of shrimp. The double-stranded RNA binding domains (dsRBDs) B and C of the TRBP from Marsupenaeus japonicus ( Mj -TRBP) were found to mediate the interaction of TRBP and eIF6. Gel-shift assays revealed that the N-terminal of Mj -TRBP dsRBD strongly binds to double-stranded RNA (dsRNA) and that the homodimer of the TRBP mediated by the C-terminal dsRBD increases the affinity to dsRNA. RNAi against either Mj -TRBP or Mj -eIF6 impairs the dsRNA-induced sequence-specific RNAi pathway and facilitates the proliferation of white spot syndrome virus (WSSV). These results further proved the important roles of TRBP and eIF6 in the antiviral response of shrimp.
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titleTRBP and eIF6 Homologue in Marsupenaeus japonicus Play Crucial Roles in Antiviral Response (TRBP and eIF6 in Antiviral Response)
descriptionPlants and invertebrates can suppress viral infection through RNA silencing, mediated by RNA-induced silencing complex (RISC). Trans-activation response RNA-binding protein (TRBP), consisting of three double-stranded RNA-binding domains, is a component of the RISC. In our previous paper, a TRBP homologue in Fenneropenaeus chinensis ( Fc -TRBP) was reported to directly bind to eukaryotic initiation factor 6 ( Fc -eIF6). In this study, we further characterized the function of TRBP and the involvement of TRBP and eIF6 in antiviral RNA interference (RNAi) pathway of shrimp. The double-stranded RNA binding domains (dsRBDs) B and C of the TRBP from Marsupenaeus japonicus ( Mj -TRBP) were found to mediate the interaction of TRBP and eIF6. Gel-shift assays revealed that the N-terminal of Mj -TRBP dsRBD strongly binds to double-stranded RNA (dsRNA) and that the homodimer of the TRBP mediated by the C-terminal dsRBD increases the affinity to dsRNA. RNAi against either Mj -TRBP or Mj -eIF6 impairs the dsRNA-induced sequence-specific RNAi pathway and facilitates the proliferation of white spot syndrome virus (WSSV). These results further proved the important roles of TRBP and eIF6 in the antiviral response of shrimp.
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abstractPlants and invertebrates can suppress viral infection through RNA silencing, mediated by RNA-induced silencing complex (RISC). Trans-activation response RNA-binding protein (TRBP), consisting of three double-stranded RNA-binding domains, is a component of the RISC. In our previous paper, a TRBP homologue in Fenneropenaeus chinensis ( Fc -TRBP) was reported to directly bind to eukaryotic initiation factor 6 ( Fc -eIF6). In this study, we further characterized the function of TRBP and the involvement of TRBP and eIF6 in antiviral RNA interference (RNAi) pathway of shrimp. The double-stranded RNA binding domains (dsRBDs) B and C of the TRBP from Marsupenaeus japonicus ( Mj -TRBP) were found to mediate the interaction of TRBP and eIF6. Gel-shift assays revealed that the N-terminal of Mj -TRBP dsRBD strongly binds to double-stranded RNA (dsRNA) and that the homodimer of the TRBP mediated by the C-terminal dsRBD increases the affinity to dsRNA. RNAi against either Mj -TRBP or Mj -eIF6 impairs the dsRNA-induced sequence-specific RNAi pathway and facilitates the proliferation of white spot syndrome virus (WSSV). These results further proved the important roles of TRBP and eIF6 in the antiviral response of shrimp.
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doi10.1371/journal.pone.0030057
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date2012-01-18