The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

Xue, Qiao; Liu, Huisheng; Zeng, Qiaoying; Zheng, Haixue; Xue, Qinghong; Cai, Xuepeng

doi:10.1007/s12250-019-00148-7

Cited by 23 publications

(25 citation statements)

References 38 publications

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“…DDX1 is another stress granule resident protein [12] and has been found to inhibit or facilitate diverse viral infections including HIV, foot and mouth disease virus (FMDV), and transmissible gastroenteritis virus [18,71,75,76]. DDX1 was identified in a two-hybrid screen for HIV-Rev interactors and was shown to modulate the localization of Rev and the splicing of HIV mRNA.…”

Section: P-body and Stress Granule Helicases In Viral Infectionmentioning

confidence: 99%

“…Moreover, in a yeast model of Tombus virus infection, Ded1 and Dbp2 enhance viral replication by unwinding 3 secondary structure to promote plus-strand RNA synthesis [82]. DDX1 inhibits foot and mouth disease virus and increases IFNβ production in infected cells [76]. DDX1 acts as a coactivator of NF-κB-mediated transcription via interaction with RelA, a function which requires intact helicase activity [19].…”

Section: P-body and Stress Granule Helicases In Viral Infectionmentioning

confidence: 99%

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DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense

Taschuk

Cherry

2020

Viruses

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DEAD-box helicases are a large family of conserved RNA-binding proteins that belong to the broader group of cellular DExD/H helicases. Members of the DEAD-box helicase family have roles throughout cellular RNA metabolism from biogenesis to decay. Moreover, there is emerging evidence that cellular RNA helicases, including DEAD-box helicases, play roles in the recognition of foreign nucleic acids and the modulation of viral infection. As intracellular parasites, viruses must evade detection by innate immune sensing mechanisms and degradation by cellular machinery while also manipulating host cell processes to facilitate replication. The ability of DEAD-box helicases to recognize RNA in a sequence-independent manner, as well as the breadth of cellular functions carried out by members of this family, lead them to influence innate recognition and viral infections in multiple ways. Indeed, DEAD-box helicases have been shown to contribute to intracellular immune sensing, act as antiviral effectors, and even to be coopted by viruses to promote their replication. However, our understanding of the mechanisms underlying these interactions, as well as the cellular roles of DEAD-box helicases themselves, is limited in many cases. We will discuss the diverse roles that members of the DEAD-box helicase family play during viral infections.Viruses 2020, 12, 181 2 of 15 helicases to particular RNAs or proteins; the diversity of these regions accounts for the breadth of function observed within this protein family [7]. As a result of their diversity of binding and function, DEAD-box RNA helicases are involved in all aspects of cellular RNA metabolism, including transcription, splicing, microRNA biogenesis, ribosomal RNA processing, RNA export, translation, RNP granule formation, and decay [10]. Moreover, they are also involved in cellular stress responses, contributing to double-strand break (DSB) repair [11], stress granule formation, and antimicrobial responses [12]. DEAD-Box Helicases in Canonical Innate Immune SensingInnate immune defenses depend upon the recognition of invading pathogens by the host, and viral infections, including RNA viruses, are largely sensed through nucleic acid recognition. RNA viruses present a host cell with various foreign RNA features, such as unique ends, structured RNA elements, or dsRNA replication intermediates, which can be recognized as hallmarks of infection. RNA binding proteins thus play important roles in the sensing of viral infection, and DExD/H helicases are well-suited to recognize structural features characteristic of viral RNAs.The canonical cytoplasmic sensors of viral RNA, the RIG-I-like receptors (RLRs) RIG-I and MDA-5, contain DExD/H-box helicase domains [13]. RIG-I recognizes uncapped viral RNAsand short dsRNAs containing a 5 triphosphate, while MDA-5 binds longer dsRNA replication intermediates [13][14][15]. In addition to the helicase core domain, these proteins contain caspase activation and recruitment domains (CARDs).RNA recognition by these RLRs leads to oligomerization of ...

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Section: P-body and Stress Granule Helicases In Viral Infectionmentioning

confidence: 99%

Section: P-body and Stress Granule Helicases In Viral Infectionmentioning

confidence: 99%

DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense

Taschuk

Cherry

2020

Viruses

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“…Another gene DDX1 on BTA11 was reported to be involved in bovine mammary involution in environmental stress conditions (Dado-Senn et al, 2018). DDX1 is also reported to be associated with linoleic acid content in Nellore cattle (Lemos et al, 2016) and viral resistance (Xue et al,2019).…”

Section: Discussionmentioning

confidence: 99%

Signatures of Selection in CompositeVrindavaniCattle of India

Singh

Mehrotra

Gondro

et al. 2020

Preprint

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Vrindavani is an Indian composite cattle breed developed by crossbreeding taurine dairy breeds with native insicine cattle in the 1960s. About 190,000 semen doses of Vrindavni bulls have been distributed to the farmer till date. the animals are under artificial and natural selection for higher milk production and adaptation traits in the Vrindavani genome is not explored. In this study, we provide the first overview of the selection signatures in Vrindavani genome. 96 Vrindavani cattle were genotyped using BovineSNP BeadChip and the SNP genotype data of its constituent breeds were collected from a public database. Within-breed selection signatures in VRindavani were investigted using the integrated haplotype score. Vrindavani was also compared to each of its parental breeds to discover between-population signature of selection using two approaches, cross population extended haplotype homozygosity and fixation index. Signature of selection identifies 11 common region identified by more than one mthod harbouring gene such as LRP1B, TNN13K, APOB, CACNA2D1, FAM110B and SPATA17 associated with production and adaptation. Overall, our results suggest stronger selection pressure on regions responsible for adaptation compared to milk yield.

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“…Further study has indicated that 2C and Nmi induce a type I IFN response, and expression of FMDV 2C or Nmi significantly suppresses VSV replication ( Zheng et al, 2014 ). In addition, 3D pol interacts with DEAD-box RNA helicase 1 (DDX1), which has been identified to inhibit FMDV replication due to its ATPase or helicase activity and induce the production of host IFN-β protein to enhance antiviral innate immunity ( Xue et al, 2019 ). In addition, the non-coding regions (i.e., 5′ Grubman and Baxt, 2004 ).…”

Section: Fmdv Proteins Regulate Host Innate Immunitymentioning

confidence: 99%

Advances in Foot-and-Mouth Disease Virus Proteins Regulating Host Innate Immunity

Peng

Yang

et al. 2020

Front. Microbiol.

Self Cite

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Foot-and-mouth disease (FMD) is a highly contagious disease that affects cloven-hoofed animals such as pigs, cattle, and sheep. The disease is caused by the foot-and-mouth disease virus (FMDV) which has a non-enveloped virion with icosahedral symmetry that encapsulates a positive-sense, single-stranded RNA genome of ∼8.4 kb. FMDV infection causes obvious immunosuppressive effects on the host. In recent years, studies on the immunosuppressive mechanism of FMDV have become a popular topic. In addition, studies have shown that many FMDV proteins are involved in the regulation of host innate immunity and have revealed mechanisms by which FMDV proteins mediate host innate immunity. In this review, advances in studies on the mechanisms of interaction between FMDV proteins and host innate immunity are summarized to provide a comprehensive understanding of FMDV pathogenesis and the theoretical basis for FMD prevention and control.

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The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

Cited by 23 publications

References 38 publications

DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense

DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense

Signatures of Selection in CompositeVrindavaniCattle of India

Advances in Foot-and-Mouth Disease Virus Proteins Regulating Host Innate Immunity

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