Aquatic viruses induce host cell death pathways and its application

Reshi, Latif; Wu, Jen Leih; Wang, Hao Ven; Hong, Jiann Ruey

doi:10.1016/j.virusres.2015.10.018

Cited by 38 publications

(35 citation statements)

References 152 publications

(151 reference statements)

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“…To date, significant research on aquatic viruses and fish immune responses against the pathogens has been performed; however, little is known about the evasion mechanisms of aquatic viruses from the fish immune system (30). Here, we report that the SVCV P protein, as a substrate of fish TBK1, competes with IRF3 for phosphorylation, leading to the reduction of IRF3 phosphorylation and IFN transcription.…”

Section: Discussionmentioning

confidence: 85%

The P Protein of Spring Viremia of Carp Virus Negatively Regulates the Fish Interferon Response by Inhibiting the Kinase Activity of TANK-Binding Kinase 1

Wang

et al. 2016

J Virol

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Spring viremia of carp virus (SVCV) is an efficient pathogen causing high mortality in the common carp. Fish interferon (IFN) is a powerful cytokine enabling host cells to establish an antiviral response; therefore, the strategies that SVCV uses to avoid the cellular IFN response were investigated. Here, we report that the SVCV P protein is phosphorylated by cellular TANK-binding kinase 1 (TBK1), which decreases IFN regulatory factor 3 (IRF3) phosphorylation and suppresses IFN production. First, overexpression of P protein inhibited the IFN promoter activation induced by SVCV and the IFN activity activated by the mitochondrial antiviral signaling protein (MAVS) although TBK1 activity was not blocked by P protein. Second, P protein colocalized and interacted with TBK1. Dominant negative experiments suggested that the TBK1 N-terminal kinase domain interacted with P protein and was essential for P protein and IRF3 phosphorylation. Finally, P protein overexpression reduced the IRF3 phosphorylation activated by TBK1 and reduced host cellular ifn transcription. Collectively, our data demonstrated that the SVCV P protein is a decoy substrate for the host phosphokinase TBK1, preventing IFN production and facilitating SVCV replication. IMPORTANCETBK1 is a pivotal phosphokinase that activates host IFN production to defend against viral infection; thus, it is a potential target for viruses to negatively regulate IFN response and facilitate viral evasion. We report that the SVCV P protein functions as a decoy substrate for cellular TBK1, leading to the reduction of IRF3 phosphorylation and suppression of IFN expression. These findings reveal a novel immune evasion mechanism of SVCV. In aquatic viruses, spring viremia of carp virus (SVCV) belongs to the genus Vesiculovirus of the family Rhabdoviridae and causes significant mortality in the common carp (Cyprinus carpio) (1). Regarding its genome structure, SVCV encodes an ϳ11-kb negative-sense, single-stranded RNA that encodes five proteins in the following order (3= to 5=): nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and viral RNA-dependent RNA polymerase (L) (2-4). The roles of these proteins in the replication and proliferation of rhabdovirus have been explored. N protein associates with viral RNA to form the nucleocapsid during viral assembly. M protein participates in the assembly and budding of virus, and G protein is involved in viral endocytosis. Moreover, as a phosphoprotein, the P protein is involved in several viral replication and assembly processes. As an example, the functional phosphorylated P protein interacts with the L protein to form a viral polymerase complex that interacts with the RNA template. In addition, the P protein also maintains the N protein in a soluble, encapsidation-competent form (1, 5).In host cells, viral RNAs can be recognized by the cellular immune system, triggering an antiviral response (6). In the cytoplasm, RIG-I-like receptors (RLRs), including RIG-I and MDA5, are the major pattern-recognition...

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Section: Discussionmentioning

confidence: 85%

The P Protein of Spring Viremia of Carp Virus Negatively Regulates the Fish Interferon Response by Inhibiting the Kinase Activity of TANK-Binding Kinase 1

Wang

et al. 2016

J Virol

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“…Although the first AUG of S9 segment appears to be not in a very favorable context for initiation of translation (UGUAUGG) according to the consensus sequence (A/G)NNAUGG (N = any nucleoside), in most cases, the AUG nearest the 5 0 -terminal cap is exclusively used for initiation for protein synthesis in a ''scanning model'' [15,16]. The putative methionine start codon (nucleotides [23][24][25] is thus the first triplet rather than the others.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, GCRV is also fatal to various aquatic animals including rare minnow (Gobiocypris rarus), black carp (Mylopharyngodon piceus), and topmouth gudeon (Pseudorasbora parva) [26]. It has been suggested that globalization of aquaculture operations has apparently accelerated the spread of GCRV [24]. GCRV is composed of 11 double-stranded RNA (dsRNA) segments and belongs to genus Aquareovirus (AQRV), family Reoviridae.…”

Section: Introductionmentioning

confidence: 99%

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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“…However, the aquaculture production rate of abalone has been decreasing recently, possibly due to several reasons, such as deterioration of aquaculture environments, genetic degradation, and diseases (2). A variety of marine viruses cause significant economic losses in an aquaculture species (3, 4). Until now, only abalone herpesviruses have been confirmed as the causative agents of the disease observed in farmed abalone (5).…”

Section: Genome Announcementmentioning

confidence: 99%

Genome Sequences of a Novel Picorna-Like Virus from Pacific Abalone ( Haliotis discus hannai ) in South Korea

et al. 2017

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We report the draft genome sequences of a novel member of the Picornavirales isolated from Pacific abalone (Haliotis discus hannai). The full length of the assembled draft genome sequences, obtained by use of a next-generation sequencing technique, were 8,019 nucleotides, including an RNA-dependent RNA polymerase gene (5,088 nucleotides) and a capsid protein gene (2,553 nucleotides). This genome sequence will be useful for understanding viral disease of Pacific abalone.

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Aquatic viruses induce host cell death pathways and its application

Cited by 38 publications

References 152 publications

The P Protein of Spring Viremia of Carp Virus Negatively Regulates the Fish Interferon Response by Inhibiting the Kinase Activity of TANK-Binding Kinase 1

The P Protein of Spring Viremia of Carp Virus Negatively Regulates the Fish Interferon Response by Inhibiting the Kinase Activity of TANK-Binding Kinase 1

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

Genome Sequences of a Novel Picorna-Like Virus from Pacific Abalone ( Haliotis discus hannai ) in South Korea

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