title: TRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral response.
abstract: 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.
authors.affiliation: The Key Laboratory of Plant Cell Engineering and Germplasm Innovation of Ministry of Education, School of Life Sciences, Shandong University, Jinan, Shandong, People's Republic of China.
authors.forename: Shuai
authors.initials: S
authors.lastname: Wang
authors.forename: An-Jing
authors.initials: AJ
authors.lastname: Chen
authors.forename: Li-Jie
authors.initials: LJ
authors.lastname: Shi
authors.forename: Xiao-Fan
authors.initials: XF
authors.lastname: Zhao
authors.forename: Jin-Xing
authors.initials: JX
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D024202:Electrophoretic Mobility Shift Assay; D054884:Host-Pathogen Interactions; D008969:Molecular Sequence Data; D033561:Penaeidae / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D010448:Peptide Initiation Factors / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D034622:RNA Interference; D012330:RNA, Double-Stranded / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D034743:RNA-Induced Silencing Complex / Q000235:genetics / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014779:Virus Replication / Q000235:genetics; D046848:White spot syndrome virus 1 / Q000235:genetics / Q000502:physiology; D000099253:Trans-Activation Responsive RNA-Binding Protein
chemical_list: D010448:Peptide Initiation Factors; D020033:Protein Isoforms; D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; D034743:RNA-Induced Silencing Complex; D000099253:Trans-Activation Responsive RNA-Binding Protein; C021019:eIF-6