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Journal articles on the topic 'An RNase active on dsRNA'

Author: Grafiati

Published: 11 March 2023

Last updated: 31 July 2025

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1

Weinheimer, Isabel, Kajohn Boonrod, Mirko Moser, et al. "Binding and processing of small dsRNA molecules by the class 1 RNase III protein encoded by sweet potato chlorotic stunt virus." Journal of General Virology 95, no. 2 (2014): 486–95. http://dx.doi.org/10.1099/vir.0.058693-0.

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Sweet potato chlorotic stunt virus (SPCSV; genus Crinivirus, family Closteroviridae) causes heavy yield losses in sweet potato plants co-infected with other viruses. The dsRNA-specific class 1 RNase III–like endoribonuclease (RNase3) encoded by SPCSV suppresses post-transcriptional gene silencing and eliminates antiviral defence in sweet potato plants in an endoribonuclease activity-dependent manner. RNase3 can cleave long dsRNA molecules, synthetic small interfering RNAs (siRNAs), and plant- and virus-derived siRNAs extracted from sweet potato plants. In this study, conditions for efficient e

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2

Iqbal, Munir, Emma Poole, Stephen Goodbourn, and John W. McCauley. "Role for Bovine Viral Diarrhea Virus Erns Glycoprotein in the Control of Activation of Beta Interferon by Double-Stranded RNA." Journal of Virology 78, no. 1 (2004): 136–45. http://dx.doi.org/10.1128/jvi.78.1.136-145.2004.

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ABSTRACT Production of alpha/beta interferon in response to viral double-stranded RNA (dsRNA) produced during viral replication is a first line of defense against viral infections. Here we demonstrate that the Erns glycoprotein of the pestivirus bovine viral diarrhea virus can act as an inhibitor of dsRNA-induced responses of cells. This effect is seen whether Erns is constitutively expressed in cells or exogenously added to the culture medium. The Erns effect is specific to dsRNA since activation of NF-κB in cells infected with Semliki Forest virus or treated with tumor necrosis factor alpha

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3

Gupta, Ankush, and Pramod C. Rath. "Curcumin, a Natural Antioxidant, Acts as a Noncompetitive Inhibitor of Human RNase L in Presence of Its Cofactor 2-5AIn Vitro." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/817024.

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Ribonuclease L (RNase L) is an antiviral endoribonuclease of the innate immune system, which is induced and activated by viral infections, interferons, and double stranded RNA (dsRNA) in mammalian cells. Although, RNase L is generally protective against viral infections, abnormal RNase L expression and activity have been associated with a number of diseases. Here, we show that curcumin, a natural plant-derived anti-inflammatory active principle, inhibits RNase L activity; hence, it may be exploited for therapeutic interventions in case of pathological situations associated with excess activati

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4

Li, Yize, Shuvojit Banerjee, Yuyan Wang, et al. "Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses." Proceedings of the National Academy of Sciences 113, no. 8 (2016): 2241–46. http://dx.doi.org/10.1073/pnas.1519657113.

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The 2′,5′-oligoadenylate (2-5A) synthetase (OAS)–RNase L system is an IFN-induced antiviral pathway. RNase L activity depends on 2-5A, synthesized by OAS. Although all three enzymatically active OAS proteins in humans—OAS1, OAS2, and OAS3—synthesize 2-5A upon binding dsRNA, it is unclear which are responsible for RNase L activation during viral infection. We used clustered regularly interspaced short palindromic repeats (CRISPR)–CRISPR-associated protein-9 nuclease (Cas9) technology to engineer human A549-derived cell lines in which each of the OAS genes or RNase L is knocked out. Upon transfe

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5

Grünberg, Sebastian, Baptiste Coxam, Tien-Hao Chen, et al. "E. coli RNase I exhibits a strong Ca2+-dependent inherent double-stranded RNase activity." Nucleic Acids Research 49, no. 9 (2021): 5265–77. http://dx.doi.org/10.1093/nar/gkab284.

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Abstract Since its initial characterization, Escherichia coli RNase I has been described as a single-strand specific RNA endonuclease that cleaves its substrate in a largely sequence independent manner. Here, we describe a strong calcium (Ca2+)-dependent activity of RNase I on double-stranded RNA (dsRNA), and a Ca2+-dependent novel hybridase activity, digesting the RNA strand in a DNA:RNA hybrid. Surprisingly, Ca2+ does not affect the activity of RNase I on single stranded RNA (ssRNA), suggesting a specific role for Ca2+ in the modulation of RNase I activity. Mutation of a previously overlooke

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6

Weiss, Susan R. "Activation and Antagonism of the OAS–RNase L Pathway." Proceedings 50, no. 1 (2020): 14. http://dx.doi.org/10.3390/proceedings2020050014.

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The oligoadenylate synthetase–ribonuclease L (OAS–RNase L) system is a potent antiviral pathway that severely limits the pathogenesis of many viruses. Upon sensing dsRNA, OASs produce 2′,5′-oligoadenylates (2-5A) that activate RNase L to cleave both host and viral single-stranded RNA, thereby limiting protein production, virus replication and spread, leading to apoptotic cell death. Endogenous host dsRNA, which accumulates in the absence of adenosine deaminase acting on RNA (ADAR)1, can also activate RNase L and lead to apoptotic cell death. RNase L activation and antiviral activity during inf

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7

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum

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8

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum

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9

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum

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10

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum

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11

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum

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12

Magkouras, Ioannis, Philippe Mätzener, Till Rümenapf, Ernst Peterhans, and Matthias Schweizer. "RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses." Journal of General Virology 89, no. 10 (2008): 2501–6. http://dx.doi.org/10.1099/vir.0.2008/003749-0.

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Recombinant pestivirus envelope glycoprotein Erns has been shown to interfere with dsRNA-induced interferon (IFN-α/β) synthesis. This study demonstrated that authentic, enzymically active Erns produced in mammalian cells prevented a dsRNA-induced IFN response when present in the supernatant of bovine cells. Strikingly, IFN synthesis of cells expressing Erns was eliminated after extracellular addition, but not transfection, of dsRNA. Importantly, the same applied to cells infected with bovine viral diarrhea virus (BVDV) expressing Erns but lacking the N-terminal protease Npro. Free Erns concent

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13

Boyce, Mark, and Polly Roy. "Recovery of Infectious Bluetongue Virus from RNA." Journal of Virology 81, no. 5 (2006): 2179–86. http://dx.doi.org/10.1128/jvi.01819-06.

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ABSTRACT Bluetongue virus (BTV) is an insect-vectored emerging pathogen of ruminants with the potential for devastating economic impact on European agriculture. BTV and many other members of the Reoviridae have remained stubbornly refractory to the development of methods for the rescue of infectious virus from cloned nucleic acid (reverse genetics). Partially disassembled virus particles are transcriptionally active, synthesizing viral transcripts in the cytoplasm of infected cells, in essence delivering viral nucleic acids in situ. With the goal of generating a reverse-genetics system for BTV

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14

Askenase, Philip. "Suppressor T cell exosomes via miR-150* and antigen specific Ig light chains. (50.13)." Journal of Immunology 186, no. 1_Supplement (2011): 50.13. http://dx.doi.org/10.4049/jimmunol.186.supp.50.13.

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Abstract Tolerance in contact sensitivity (CS) is due to CD8+ suppressor T cell (Ts) released factor (TsF) that is phenol chloroform extractable (PCE), in RNA fraction of Qiagen DNA/RNA separation column, sensitive to RNase A, not DNase nor trypsin, and also sensitive to RNase III; a property of double stranded RNA (dsRNA) like miRNA. Sizing electrophoresis indicated the active inhibitory RNA was about 75bp; the size of pre-miRNA. TsF RNA also inhibited in vitro IL-2 responses of T cell lines. We concluded that the small suppressive dsRNA was in the miRNA family TsF RNA is transported systemat

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15

Tian, Lan, Min-Sung Kim, Hongzhi Li, Jimin Wang, and Wei Yang. "Structure of HIV-1 reverse transcriptase cleaving RNA in an RNA/DNA hybrid." Proceedings of the National Academy of Sciences 115, no. 3 (2018): 507–12. http://dx.doi.org/10.1073/pnas.1719746115.

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HIV-1 reverse transcriptase (RT) contains both DNA polymerase and RNase H activities to convert the viral genomic RNA to dsDNA in infected host cells. Here we report the 2.65-Å resolution structure of HIV-1 RT engaging in cleaving RNA in an RNA/DNA hybrid. A preferred substrate sequence is absolutely required to enable the RNA/DNA hybrid to adopt the distorted conformation needed to interact properly with the RNase H active site in RT. Substituting two nucleotides 4 bp upstream from the cleavage site results in scissile-phosphate displacement by 4 Å. We also have determined the structure of HI

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16

von Beck, Troy Alexander, Luis Mena Hernandez, Hongyi Zhou, Jeffrey Skolnick, and Joshy Jacob. "Repurposed antibiotic and antiviral drugs inhibit the immune evasive endoribonuclease of SARS-CoV-2 and restrict coronavirus infection in vitro." Journal of Immunology 208, no. 1_Supplement (2022): 125.29. http://dx.doi.org/10.4049/jimmunol.208.supp.125.29.

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Abstract Despite the success of SARS-CoV-2 vaccines in curbing viral transmission and severe disease, infections in unvaccinated and immune deficient patients continue to drive significant morbidity and mortality globally. To address the needs of this patient population, multiple antiviral drugs must be developed to expand on the protection currently offered by convalescent plasma, monoclonal antibodies, remdesivir, and other next generation SARS-CoV-2 antivirals which may be contraindicated for some patient groups. To this end, we employed a machine-learning based virtual ligand screening alg

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17

Gao, Yanning, Shao-an Xue, and Beverly E. Griffin. "Sensitivity of an Epstein-Barr Virus-Positive Tumor Line, Daudi, to Alpha Interferon Correlates with Expression of a GC-Rich Viral Transcript." Molecular and Cellular Biology 19, no. 11 (1999): 7305–13. http://dx.doi.org/10.1128/mcb.19.11.7305.

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ABSTRACT The exquisite sensitivity of the Burkitt’s lymphoma (BL)-derived cell line Daudi to type I interferons has not previously been explained. Here we show that expression of an Epstein-Barr virus (EBV) transcript, designated D-HIT (Y. Gao et al., J. Virol. 71:84–94, 1997), correlates with the sensitivity of different Daudi cell isolates (or that of other EBV-carrying cells, where known) to alpha interferon (IFN-α). D-HIT, transcribed from a GC-rich repetitive region (IR4) of the viral genome, is highly structured, responding to RNase digestion in a manner akin to double-stranded RNA. Comp

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18

Iordanov, Mihail S., Jayashree M. Paranjape, Aimin Zhou, et al. "Activation of p38 Mitogen-Activated Protein Kinase and c-Jun NH2-Terminal Kinase by Double-Stranded RNA and Encephalomyocarditis Virus: Involvement of RNase L, Protein Kinase R, and Alternative Pathways." Molecular and Cellular Biology 20, no. 2 (2000): 617–27. http://dx.doi.org/10.1128/mcb.20.2.617-627.2000.

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ABSTRACT Double-stranded RNA (dsRNA) accumulates in virus-infected mammalian cells and signals the activation of host defense pathways of the interferon system. We describe here a novel form of dsRNA-triggered signaling that leads to the stimulation of the p38 mitogen-activated protein kinase (p38 MAPK) and the c-Jun NH2-terminal kinase (JNK) and of their respective activators MKK3/6 and SEK1/MKK4. The dsRNA-dependent signaling to p38 MAPK was largely intact in cells lacking both RNase L and the dsRNA-activated protein kinase (PKR), i.e., the two best-characterized mediators of dsRNA-triggered

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19

Nameth, S. T., and S. L. Cheng. "Identification and Partial Characterization of Endogenous Double-stranded Ribonucleic Acid in Mulberry." Journal of the American Society for Horticultural Science 119, no. 4 (1994): 859–61. http://dx.doi.org/10.21273/jashs.119.4.859.

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Double-stranded ribonucleic acid (dsRNA) analysis of apparently healthy red mulberry (Morus rubra L.) yielded four distinct dsRNA banding profiles. dsRNA type 1 contained three dsRNA bands with approximate molecular weights (MWs) of 12.0, 1.0, and 0.9 × 106, respectively. dsRNA type 2 contained two dsRNA bands with MWs of 1.0 and 0.9 × 106. dsRNA type 3 contained four dsRNA bands with MWs of 1.0, 0.9, 0.89, and 0.88 × 106. dsRNA type 4 contained three dsRNA bands with MWs of 1.0, 0.88, and 0.87 × 106. No virus particles were associated with any of the samples analyzed. All four types of dsRNA

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20

Cánovas-Márquez, José Tomás, Sebastian Falk, Francisco E. Nicolás, et al. "A ribonuclease III involved in virulence of Mucorales fungi has evolved to cut exclusively single-stranded RNA." Nucleic Acids Research 49, no. 9 (2021): 5294–307. http://dx.doi.org/10.1093/nar/gkab238.

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Abstract Members of the ribonuclease III (RNase III) family regulate gene expression by processing double-stranded RNA (dsRNA). This family includes eukaryotic Dicer and Drosha enzymes that generate small dsRNAs in the RNA interference (RNAi) pathway. The fungus Mucor lusitanicus, which causes the deadly infection mucormycosis, has a complex RNAi system encompassing a non-canonical RNAi pathway (NCRIP) that regulates virulence by degrading specific mRNAs. In this pathway, Dicer function is replaced by R3B2, an atypical class I RNase III, and small single-stranded RNAs (ssRNAs) are produced ins

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21

Kreuze, Jan F., Eugene I. Savenkov, Wilmer Cuellar, Xiangdong Li, and Jari P. T. Valkonen. "Viral Class 1 RNase III Involved in Suppression of RNA Silencing." Journal of Virology 79, no. 11 (2005): 7227–38. http://dx.doi.org/10.1128/jvi.79.11.7227-7238.2005.

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ABSTRACT Double-stranded RNA (dsRNA)-specific endonucleases belonging to RNase III classes 3 and 2 process dsRNA precursors to small interfering RNA (siRNA) or microRNA, respectively, thereby initiating and amplifying RNA silencing-based antiviral defense and gene regulation in eukaryotic cells. However, we now provide evidence that a class 1 RNase III is involved in suppression of RNA silencing. The single-stranded RNA genome of sweet potato chlorotic stunt virus (SPCSV) encodes an RNase III (RNase3) homologous to putative class 1 RNase IIIs of unknown function in rice and Arabidopsis. We sho

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Daou, Salima, Manisha Talukdar, Jinle Tang, et al. "A phenolic small molecule inhibitor of RNase L prevents cell death from ADAR1 deficiency." Proceedings of the National Academy of Sciences 117, no. 40 (2020): 24802–12. http://dx.doi.org/10.1073/pnas.2006883117.

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The oligoadenylate synthetase (OAS)–RNase L system is an IFN-inducible antiviral pathway activated by viral infection. Viral double-stranded (ds) RNA activates OAS isoforms that synthesize the second messenger 2-5A, which binds and activates the pseudokinase-endoribonuclease RNase L. In cells, OAS activation is tamped down by ADAR1, an adenosine deaminase that destabilizes dsRNA. Mutation of ADAR1 is one cause of Aicardi-Goutières syndrome (AGS), an interferonopathy in children. ADAR1 deficiency in human cells can lead to RNase L activation and subsequent cell death. To evaluate RNase L as a p

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Banerjee, Shuvojit, Elona Gusho, Christina Gaughan, et al. "OAS-RNase L innate immune pathway mediates the cytotoxicity of a DNA-demethylating drug." Proceedings of the National Academy of Sciences 116, no. 11 (2019): 5071–76. http://dx.doi.org/10.1073/pnas.1815071116.

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Drugs that reverse epigenetic silencing, such as the DNA methyltransferase inhibitor (DNMTi) 5-azacytidine (AZA), have profound effects on transcription and tumor cell survival. AZA is an approved drug for myelodysplastic syndromes and acute myeloid leukemia, and is under investigation for different solid malignant tumors. AZA treatment generates self, double-stranded RNA (dsRNA), transcribed from hypomethylated repetitive elements. Self dsRNA accumulation in DNMTi-treated cells leads to type I IFN production and IFN-stimulated gene expression. Here we report that cell death in response to AZA

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Chitrakar, Alisha, Sneha Rath, Jesse Donovan та ін. "Real-time 2-5A kinetics suggest that interferons β and λ evade global arrest of translation by RNase L". Proceedings of the National Academy of Sciences 116, № 6 (2019): 2103–11. http://dx.doi.org/10.1073/pnas.1818363116.

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Cells of all mammals recognize double-stranded RNA (dsRNA) as a foreign material. In response, they release interferons (IFNs) and activate a ubiquitously expressed pseudokinase/endoribonuclease RNase L. RNase L executes regulated RNA decay and halts global translation. Here, we developed a biosensor for 2′,5′-oligoadenylate (2-5A), the natural activator of RNase L. Using this biosensor, we found that 2-5A was acutely synthesized by cells in response to dsRNA sensing, which immediately triggered cellular RNA cleavage by RNase L and arrested host protein synthesis. However, translation-arrested

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Zeng, Chun, Xin Yi, Danny Zipris, et al. "RNase L contributes to experimentally induced type 1 diabetes onset in mice." Journal of Endocrinology 223, no. 3 (2014): 277–87. http://dx.doi.org/10.1530/joe-14-0509.

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The cause of type 1 diabetes continues to be a focus of investigation. Studies have revealed that interferon α (IFNα) in pancreatic islets after viral infection or treatment with double-stranded RNA (dsRNA), a mimic of viral infection, is associated with the onset of type 1 diabetes. However, how IFNα contributes to the onset of type 1 diabetes is obscure. In this study, we found that 2-5A-dependent RNase L (RNase L), an IFNα-inducible enzyme that functions in the antiviral and antiproliferative activities of IFN, played an important role in dsRNA-induced onset of type 1 diabetes. Using RNase

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Liu, Ruikang, and Bernard Moss. "Opposing Roles of Double-Stranded RNA Effector Pathways and Viral Defense Proteins Revealed with CRISPR-Cas9 Knockout Cell Lines and Vaccinia Virus Mutants." Journal of Virology 90, no. 17 (2016): 7864–79. http://dx.doi.org/10.1128/jvi.00869-16.

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ABSTRACTVaccinia virus (VACV) decapping enzymes and cellular exoribonuclease Xrn1 catalyze successive steps in mRNA degradation and prevent double-stranded RNA (dsRNA) accumulation, whereas the viral E3 protein can bind dsRNA. We showed that dsRNA and E3 colocalized within cytoplasmic viral factories in cells infected with a decapping enzyme mutant as well as with wild-type VACV and that they coprecipitated with antibody. An E3 deletion mutant induced protein kinase R (PKR) and eukaryotic translation initiation factor alpha (eIF2α) phosphorylation earlier and more strongly than a decapping enz

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Ji, Xinhua. "RNA Biogenesis: Mechanism and Evolution of RNase III." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C210. http://dx.doi.org/10.1107/s2053273314097897.

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RNase III represents a family of dsRNA-specific endoribonucleases required for RNA maturation and gene regulation. Bacterial RNase III and eukaryotic Rnt1p, Drosha, and Dicer are representative members of the family. The bacterial enzyme possesses a single RNase III domain (RIIID) followed by a dsRNA-binding domain (dsRBD); Rnt1p is defined by the presence of an N-terminal domain (NTD), a RIIID, and a dsRBD; Drosha contains N-terminal P-rich and RS-rich domains followed by two RIIIDs and a dsRBD; and Dicer possesses N-terminal helicase, DUF283, and PAZ domains followed by two RIIIDs and a dsRB

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Yan, Wei, Lang Ma, Paula Stein, et al. "Mice Deficient in Oocyte-Specific Oligoadenylate Synthetase-Like Protein OAS1D Display Reduced Fertility." Molecular and Cellular Biology 25, no. 11 (2005): 4615–24. http://dx.doi.org/10.1128/mcb.25.11.4615-4624.2005.

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ABSTRACT The double-stranded RNA (dsRNA)-induced interferon response is a defense mechanism against viral infection. Upon interferon activation by dsRNA, 2′,5′-oligoadenylate synthetase 1 (OAS1A) is induced; it binds dsRNA and converts ATP into 2′,5′-linked oligomers of adenosine (called 2-5A), which activate RNase L that in turn degrades viral and cellular RNAs. In a screen to identify oocyte-specific genes, we identified a novel murine cDNA encoding an ovary-specific 2′,5′-oligoadenylate synthetase-like protein, OAS1D, which displays 59% identity with OAS1A. OAS1D is predominantly cytoplasmi

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Azevedo, Andréia Cristiane Souza, Daniel Ricardo Sosa-Gómez, Marcos Rodrigues Faria, and Maria Helena Pelegrinelli Fungaro. "Effects of double-stranded RNA on virulence of Paecilomyces fumosoroseus (Deuteromycotina: Hyphomycetes) against the silverleaf whitefly, Bemisia tabaci strain B (Homoptera: Aleyrodidae)." Genetics and Molecular Biology 23, no. 1 (2000): 61–63. http://dx.doi.org/10.1590/s1415-47572000000100010.

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Bands of double-stranded RNA (dsRNA) were detected in three out of twelve isolates of Paecilomyces fumosoroseus. Identity of these bands was confirmed by RNAse, DNAse and S1 nuclease treatments. The cure of dsRNA for one isolate (P92) was successfully carried out for a single conidium subculture. Isogenic strains, with or without dsRNA, were submitted to virulence tests against the whitefly Bemisia tabaci strain B. In contrast to findings for some phytopathogenic fungi, these dsRNA fragments did not cause hypovirulence in P. fumosoroseus.

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Whelan, Jillian N., Nicholas A. Parenti, Joshua Hatterschide, et al. "Zika virus employs the host antiviral RNase L protein to support replication factory assembly." Proceedings of the National Academy of Sciences 118, no. 22 (2021): e2101713118. http://dx.doi.org/10.1073/pnas.2101713118.

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Infection with the flavivirus Zika virus (ZIKV) can result in tissue tropism, disease outcome, and route of transmission distinct from those of other flaviviruses; therefore, we aimed to identify host machinery that exclusively promotes the ZIKV replication cycle, which can inform on differences at the organismal level. We previously reported that deletion of the host antiviral ribonuclease L (RNase L) protein decreases ZIKV production. Canonical RNase L catalytic activity typically restricts viral infection, including that of the flavivirus dengue virus (DENV), suggesting an unconventional, p

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Streitenfeld, Hein, Amanda Boyd, John K. Fazakerley, Anne Bridgen, Richard M. Elliott, and Friedemann Weber. "Activation of PKR by Bunyamwera Virus Is Independent of the Viral Interferon Antagonist NSs." Journal of Virology 77, no. 9 (2003): 5507–11. http://dx.doi.org/10.1128/jvi.77.9.5507-5511.2003.

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ABSTRACT Double-stranded RNA (dsRNA) is a by-product of viral RNA polymerase activity, and its recognition is one mechanism by which the innate immune system is activated. Cellular responses to dsRNA include induction of alpha/beta interferon (IFN) synthesis and activation of the enzyme PKR, which exerts its antiviral effect by phosphorylating the eukaryotic initiation factor eIF-2 alpha, thereby inhibiting translation. We have recently identified the nonstructural protein NSs of Bunyamwera virus (BUNV), the prototype of the family Bunyaviridae, as a virulence factor that blocks the induction

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Lamontagne, Bruno, Annie Tremblay, and Sherif Abou Elela. "The N-Terminal Domain That Distinguishes Yeast from Bacterial RNase III Contains a Dimerization Signal Required for Efficient Double-Stranded RNA Cleavage." Molecular and Cellular Biology 20, no. 4 (2000): 1104–15. http://dx.doi.org/10.1128/mcb.20.4.1104-1115.2000.

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ABSTRACT Yeast Rnt1 is a member of the double-stranded RNA (dsRNA)-specific RNase III family identified by conserved dsRNA binding (dsRBD) and nuclease domains. Comparative sequence analyses have revealed an additional N-terminal domain unique to the eukaryotic homologues of RNase III. The deletion of this domain from Rnt1 slowed growth and led to mild accumulation of unprocessed 25S pre-rRNA. In vitro, deletion of the N-terminal domain reduced the rate of RNA cleavage under physiological salt concentration. Size exclusion chromatography and cross-linking assays indicated that the N-terminal d

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Nganvongpanit, Korakot, Heike Müller, Franca Rings, et al. "Selective degradation of maternal and embryonic transcripts in in vitro produced bovine oocytes and embryos using sequence specific double-stranded RNA." Reproduction 131, no. 5 (2006): 861–74. http://dx.doi.org/10.1530/rep.1.01040.

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RNA interference (RNAi) has been used for selective degradation of an mRNA transcript or inhibiting its translation to a functional protein in various species. Here, we applied the RNAi approach to suppress the expression of the maternal transcript C-mos and embryonic transcripts Oct-4 in bovine oocytes and embryos respectively, using microinjection of sequence-specific double-stranded RNA (dsRNA). For this, 435 bp C-mos and 341 bp Oct-4 dsRNA were synthesized and microinjected into the cytoplasm of immature oocytes and zygotes respectively. In experiment 1, immature oocytes were categorized i

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Zhang, Lin, Luxi Chen, Jing Chen, Weimin Shen, and Anming Meng. "Mini-III RNase-based dual-color system for in vivo mRNA tracking." Development 147, no. 22 (2020): dev190728. http://dx.doi.org/10.1242/dev.190728.

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ABSTRACTMini-III RNase (mR3), a member of RNase III endonuclease family, can bind to and cleave double-stranded RNAs (dsRNAs). Inactive mR3 protein without the α5β-α6 loop loses the dsRNA cleavage activity, but retains dsRNA binding activity. Here, we establish an inactive mR3-based non-engineered mR3/dsRNA system for RNA tracking in zebrafish embryos. In vitro binding experiments show that inactive Staphylococcus epidermidis mR3 (dSmR3) protein possesses the highest binding affinity with dsRNAs among mR3s from other related species, and its binding property is retained in zebrafish embryos. C

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Iordanov, Mihail S., John Wong, John C. Bell та Bruce E. Magun. "Activation of NF-κB by Double-Stranded RNA (dsRNA) in the Absence of Protein Kinase R and RNase L Demonstrates the Existence of Two Separate dsRNA-Triggered Antiviral Programs". Molecular and Cellular Biology 21, № 1 (2001): 61–72. http://dx.doi.org/10.1128/mcb.21.1.61-72.2001.

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ABSTRACT Double-stranded RNA (dsRNA) of viral origin triggers two programs of the innate immunity in virus-infected cells. One is intended to decrease the rate of host cell protein synthesis and thus to prevent viral replication. This program is mediated by protein kinase R (PKR) and by RNase L and contributes, eventually, to the self-elimination of the infected cell via apoptosis. The second program is responsible for the production of antiviral (type I) interferons and other alarmone cytokines and serves the purpose of preparing naive cells for the viral invasion. This second program require

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Catalanotto, Caterina, Massimiliano Pallotta, Paul ReFalo, et al. "Redundancy of the Two Dicer Genes in Transgene-Induced Posttranscriptional Gene Silencing in Neurospora crassa." Molecular and Cellular Biology 24, no. 6 (2004): 2536–45. http://dx.doi.org/10.1128/mcb.24.6.2536-2545.2004.

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ABSTRACT RNA interference (RNAi) in animals, cosuppression in plants, and quelling in fungi are homology-dependent gene silencing mechanisms in which the introduction of either double-stranded RNA (dsRNA) or transgenes induces sequence-specific mRNA degradation. These phenomena share a common genetic and mechanistic basis. The accumulation of short interfering RNA (siRNA) molecules that guide sequence-specific mRNA degradation is a common feature in both silencing mechanisms, as is the component of the RNase complex involved in mRNA cleavage. During RNAi in animal cells, dsRNA is processed int

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Budt, Matthias, Lars Niederstadt, Ralitsa S. Valchanova, Stipan Jonjić, and Wolfram Brune. "Specific Inhibition of the PKR-Mediated Antiviral Response by the Murine Cytomegalovirus Proteins m142 and m143." Journal of Virology 83, no. 3 (2008): 1260–70. http://dx.doi.org/10.1128/jvi.01558-08.

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ABSTRACT Double-stranded RNA (dsRNA) produced during viral infection activates several cellular antiviral responses. Among the best characterized is the shutoff of protein synthesis mediated by the dsRNA-dependent protein kinase (PKR) and the oligoadenylate synthetase (OAS)/RNase L system. As viral replication depends on protein synthesis, many viruses have evolved mechanisms for counteracting the PKR and OAS/RNase L pathways. The murine cytomegalovirus (MCMV) proteins m142 and m143 have been characterized as dsRNA binding proteins that inhibit PKR activation, phosphorylation of the translatio

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Ludwig, Holger, Yasemin Suezer, Zoe Waibler, Ulrich Kalinke, Barbara S. Schnierle, and Gerd Sutter. "Double-stranded RNA-binding protein E3 controls translation of viral intermediate RNA, marking an essential step in the life cycle of modified vaccinia virus Ankara." Journal of General Virology 87, no. 5 (2006): 1145–55. http://dx.doi.org/10.1099/vir.0.81623-0.

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Infection of human cells with modified vaccinia virus Ankara (MVA) activates the typical cascade-like pattern of viral early-, intermediate- and late-gene expression. In contrast, infection of human HeLa cells with MVA deleted of the E3L gene (MVA-ΔE3L) results in high-level synthesis of intermediate RNA, but lacks viral late transcription. The viral E3 protein is thought to bind double-stranded RNA (dsRNA) and to act as an inhibitor of dsRNA-activated 2′-5′-oligoadenylate synthetase (2′-5′OA synthetase)/RNase L and protein kinase (PKR). Here, it is demonstrated that viral intermediate RNA can

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Patterson, N. A., and M. Kapoor. "Detection of plasmid-like DNA and double-stranded RNA elements in some Canadian isolates of the oilseed rape pathogen Leptosphaeria maculans." Canadian Journal of Microbiology 42, no. 9 (1996): 977–82. http://dx.doi.org/10.1139/m96-126.

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Nine Canadian isolates of Leptosphaeria maculans were examined for the presence of plasmid-like elements. A single extrachromosomal DNA element, with an estimated size of 9 kb, was detected in undigested genomic DNA of a virulent isolate, Fairview 1. This element was susceptible to hydrolysis by DNAse I and exonuclease III, and it was shown to hybridize to DNA of all virulent isolates. In addition, another virulent strain, Saskatoon 8, was observed to contain four double-stranded RNA (dsRNA) segments, ranging from approximately 500 bp to 2.4 kb. The latter segments (dsRNA) were resistant to DN

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Magg, Thomas, Tsubasa Okano, Lars M. Koenig, et al. "Heterozygous OAS1 gain-of-function variants cause an autoinflammatory immunodeficiency." Science Immunology 6, no. 60 (2021): eabf9564. http://dx.doi.org/10.1126/sciimmunol.abf9564.

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Analysis of autoinflammatory and immunodeficiency disorders elucidates human immunity and fosters the development of targeted therapies. Oligoadenylate synthetase 1 is a type I interferon–induced, intracellular double-stranded RNA (dsRNA) sensor that generates 2′-5′-oligoadenylate to activate ribonuclease L (RNase L) as a means of antiviral defense. We identified four de novo heterozygous OAS1 gain-of-function variants in six patients with a polymorphic autoinflammatory immunodeficiency characterized by recurrent fever, dermatitis, inflammatory bowel disease, pulmonary alveolar proteinosis, an

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Rath, Sneha, Jesse Donovan, Gena Whitney, Alisha Chitrakar, Wei Wang, and Alexei Korennykh. "Human RNase L tunes gene expression by selectively destabilizing the microRNA-regulated transcriptome." Proceedings of the National Academy of Sciences 112, no. 52 (2015): 15916–21. http://dx.doi.org/10.1073/pnas.1513034112.

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Double-stranded RNA (dsRNA) activates the innate immune system of mammalian cells and triggers intracellular RNA decay by the pseudokinase and endoribonuclease RNase L. RNase L protects from pathogens and regulates cell growth and differentiation by destabilizing largely unknown mammalian RNA targets. We developed an approach for transcriptome-wide profiling of RNase L activity in human cells and identified hundreds of direct RNA targets and nontargets. We show that this RNase L-dependent decay selectively affects transcripts regulated by microRNA (miR)-17/miR-29/miR-200 and other miRs that fu

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Burke, James M., Evan T. Lester, Devin Tauber, and Roy Parker. "RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules." Journal of Biological Chemistry 295, no. 6 (2020): 1426–38. http://dx.doi.org/10.1074/jbc.ra119.011638.

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Stress granules (SGs) are ribonucleoprotein (RNP) assemblies that form in eukaryotic cells as a result of limited translation in response to stress. SGs form during viral infection and are thought to promote the antiviral response because many viruses encode inhibitors of SG assembly. However, the antiviral endoribonuclease RNase L also alters SG formation, whereby only small punctate SG-like bodies that we term RNase L–dependent bodies (RLBs) form during RNase L activation. How RLBs relate to SGs and their mode of biogenesis is unknown. Herein, using immunofluorescence, live-cell imaging, and

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Gestuveo, Rommel J., Rhys Parry, Laura B. Dickson, et al. "Mutational analysis of Aedes aegypti Dicer 2 provides insights into the biogenesis of antiviral exogenous small interfering RNAs." PLOS Pathogens 18, no. 1 (2022): e1010202. http://dx.doi.org/10.1371/journal.ppat.1010202.

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The exogenous small interfering RNA (exo-siRNA) pathway is a key antiviral mechanism in the Aedes aegypti mosquito, a widely distributed vector of human-pathogenic arboviruses. This pathway is induced by virus-derived double-stranded RNAs (dsRNA) that are cleaved by the ribonuclease Dicer 2 (Dcr2) into predominantly 21 nucleotide (nt) virus-derived small interfering RNAs (vsiRNAs). These vsiRNAs are used by the effector protein Argonaute 2 within the RNA-induced silencing complex to cleave target viral RNA. Dcr2 contains several domains crucial for its activities, including helicase and RNase

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Zografidis, Aris, Filip Van Nieuwerburgh, Anna Kolliopoulou, et al. "Viral Small-RNA Analysis of Bombyx mori Larval Midgut during Persistent and Pathogenic Cytoplasmic Polyhedrosis Virus Infection." Journal of Virology 89, no. 22 (2015): 11473–86. http://dx.doi.org/10.1128/jvi.01695-15.

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ABSTRACTThe lepidopteran innate immune response against RNA viruses remains poorly understood, while in other insects several studies have highlighted an essential role for the exo-RNAi pathway in combating viral infection. Here, by using deep-sequencing technology for viral small-RNA (vsRNA) assessment, we provide evidence that exo-RNAi is operative in the silkwormBombyx moriagainst both persistent and pathogenic infection ofB. moricytoplasmic polyhedrosis virus (BmCPV) which is characterized by a segmented double-stranded RNA (dsRNA) genome. Further, we show that Dicer-2 predominantly target

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Castelli, JoAnn C., Bret A. Hassel, Katherine A. Wood, et al. "A Study of the Interferon Antiviral Mechanism: Apoptosis Activation by the 2–5A System." Journal of Experimental Medicine 186, no. 6 (1997): 967–72. http://dx.doi.org/10.1084/jem.186.6.967.

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The 2–5A system contributes to the antiviral effect of interferons through the synthesis of 2–5A and its activation of the ribonuclease, RNase L. RNase L degrades viral and cellular RNA after activation by unique, 2′–5′ phosphodiester-linked, oligoadenylates [2–5A, (pp)p5′ A2′(P5′A2′)]n, n ⩾2. Because both the 2–5A system and apoptosis can serve as viral defense mechanisms and RNA degradation occurs during both processes, we investigated the potential role of RNase L in apoptosis. Overexpression of human RNase L by an inducible promoter in NIH3T3 fibroblasts decreased cell viability and trigge

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Wojnicka, Marta, Agnieszka Szczepanska, and Anna Kurzynska-Kokorniak. "Unknown Areas of Activity of Human Ribonuclease Dicer: A Putative Deoxyribonuclease Activity." Molecules 25, no. 6 (2020): 1414. http://dx.doi.org/10.3390/molecules25061414.

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The Dicer ribonuclease plays a crucial role in the biogenesis of small regulatory RNAs (srRNAs) by processing long double-stranded RNAs and single-stranded hairpin RNA precursors into small interfering RNAs (siRNAs) and microRNAs (miRNAs), respectively. Dicer-generated srRNAs can control gene expression by targeting complementary transcripts and repressing their translation or inducing their cleavage. Human Dicer (hDicer) is a multidomain enzyme comprising a putative helicase domain, a DUF283 domain, platform, a PAZ domain, a connector helix, two RNase III domains (RNase IIIa and RNase IIIb) a

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Meng, Wenzhao, and Allen W. Nicholson. "Heterodimer-based analysis of subunit and domain contributions to double-stranded RNA processing by Escherichia coli RNase III in vitro." Biochemical Journal 410, no. 1 (2008): 39–48. http://dx.doi.org/10.1042/bj20071047.

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Members of the RNase III family are the primary cellular agents of dsRNA (double-stranded RNA) processing. Bacterial RNases III function as homodimers and contain two dsRBDs (dsRNA-binding domains) and two catalytic sites. The potential for functional cross-talk between the catalytic sites and the requirement for both dsRBDs for processing activity are not known. It is shown that an Escherichia coli RNase III heterodimer that contains a single functional wt (wild-type) catalytic site and an inactive catalytic site (RNase III[E117A/wt]) cleaves a substrate with a single scissile bond with a kca

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Liu, Kaiwen, Ryota Sato, Takuma Shibata, et al. "Skewed endosomal RNA responses from TLR7 to TLR3 in RNase T2-deficient macrophages." International Immunology 33, no. 9 (2021): 479–90. http://dx.doi.org/10.1093/intimm/dxab033.

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Abstract RNase T2, a ubiquitously expressed RNase, degrades RNAs in the endosomal compartments. RNA sensors, double-stranded RNA (dsRNA)-sensing Toll-like receptor 3 (TLR3) and single-stranded RNA (ssRNA)-sensing TLR7, are localized in the endosomal compartment in mouse macrophages. We here studied the role of RNase T2 in TLR3 and TLR7 responses in macrophages. Macrophages expressed RNase T2 and a member of the RNase A family RNase 4. RNase T2 was also expressed in plasmacytoid and conventional dendritic cells. Treatment with dsRNAs or type I interferon (IFN) up-regulated expression of RNase T

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Birdwell, L. Dillon, Zachary B. Zalinger, Yize Li, et al. "Activation of RNase L by Murine Coronavirus in Myeloid Cells Is Dependent on BasalOasGene Expression and Independent of Virus-Induced Interferon." Journal of Virology 90, no. 6 (2016): 3160–72. http://dx.doi.org/10.1128/jvi.03036-15.

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ABSTRACTThe oligoadenylate synthetase (OAS)-RNase L pathway is a potent interferon (IFN)-induced antiviral activity. Upon sensing double-stranded RNA, OAS produces 2′,5′-oligoadenylates (2-5A), which activate RNase L. Murine coronavirus (mouse hepatitis virus [MHV]) nonstructural protein 2 (ns2) is a 2′,5′-phosphodiesterase (PDE) that cleaves 2-5A, thereby antagonizing RNase L activation. PDE activity is required for robust replication in myeloid cells, as a mutant of MHV (ns2H126R) encoding an inactive PDE fails to antagonize RNase L activation and replicates poorly in bone marrow-derived mac

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Głów, Dawid, Dariusz Pianka, Agata A. Sulej, et al. "Sequence-specific cleavage of dsRNA by Mini-III RNase." Nucleic Acids Research 43, no. 5 (2015): 2864–73. http://dx.doi.org/10.1093/nar/gkv009.

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