Human TLR3 recognizes dengue virus and modulates viral replication<i>in vitro</i>

Tsai, Yi‐Lin; Chang, Sui‐Yuan; Lee, Chun-Nan; Kao, Chuan-Liang

doi:10.1111/j.1462-5822.2008.01277.x

Cited by 174 publications

(154 citation statements)

References 49 publications

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“…25 We further examined the expression of pattern recognition receptors involved in DV-induced inflammatory cytokine releases, such as Toll-like receptors (TLRs), [26][27][28] …”

Section: Differential Phenotypes Of Gm-m and M-mmentioning

confidence: 99%

CLEC5A is critical for dengue virus–induced inflammasome activation in human macrophages

Wu¹,

Chen

Yang

et al. 2013

Blood

182

174

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“…25 We further examined the expression of pattern recognition receptors involved in DV-induced inflammatory cytokine releases, such as Toll-like receptors (TLRs), [26][27][28] …”

Section: Differential Phenotypes Of Gm-m and M-mmentioning

confidence: 99%

CLEC5A is critical for dengue virus–induced inflammasome activation in human macrophages

Wu¹,

Chen

Yang

et al. 2013

Blood

182

174

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“…Similarly, mice lacking TLR3 show increased viral burden and mortality to infection by a ssRNA virus, encephalomyocarditis virus (EMCV) [88]. TLR3 can also combat HCV and DENV infections (members of family Flaviviridae, positive sense ssRNA viruses) [89,90]. Sensing ssRNA viruses and generating an optimal IFN response in plasmacytoid dendritic cells is greatly dependent on TLR7 [91].…”

Section: Toll--like Receptorsmentioning

confidence: 99%

Characterization of the termini of the West Nile virus genome and their interactions with the small isoform of the 2′ 5′-oligoadenylate synthetase family

Deo

Patel

Chojnowski

et al. 2015

Journal of Structural Biology

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confirmed the specificity of the interaction. Solution conformations of both the 5'--TR RNA of WNV and OAS1 were then elucidated using small--angle x--ray scattering. I also report that the 3' terminal region (3'--TR) is able to mediate specific interaction with and activation of OAS1. Binding and kinetic experiments identified a specific stem loop within the 3'--TR that is sufficient for activation of the enzyme. The solution confirmation of the 3'--terminal region was determined by small angle X--ray scattering, and computational models suggest a conformationally restrained structure comprised of a helix and short stem loop. Structural investigation of the 3'--ii TR in complex with OAS1 is also presented. Finally, we show that genome cyclization by base pairing between the 5'--and 3'--TRs, a required step for replication, is not sufficient to protect WNV from OAS1 recognition. The purity, monodispersity and homogeneity of all samples subjected to SAXS analysis were evaluated using dynamic light scattering and/or analytical ultra--centrifuge. These data provide a framework for understanding recognition of the highly structured terminal regions of a flaviviral genome by an innate immune enzyme.iii

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“…Subsequently, IFNAR1/2 physically associates with two tyrosine kinases, namely Janus kinase 1 (JAK1) and tyrosine kinase 2 (TyK2), and this interaction results in (Tsai et al, 2009;Liang et al, 2011). The TLR3 pathway produces IRF3, which in turn transcribe the IFNs (Borden et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Structural modeling and analysis of dengue-mediated inhibition of interferon signaling pathway

Aslam¹,

Ahmad²,

Ali³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. Dengue virus (DENV) belongs to the family Flaviviridae and can cause major health problems worldwide, including dengue fever and dengue shock syndrome. DENV replicon in human cells inhibits interferon α and β with the help of its non-structural proteins. Nonstructural protein 5 (NS5) of DENV is responsible for the proteasomemediated degradation of signal transducer and activator of transcription B. Aslam et al. 4216©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (2): 4215-4237 (2015) (STAT) 2 protein, which has been implicated in the development of resistance against interferon-mediated antiviral effect. This degradation of STAT2 primarily occurs with the help of E3 ubiquitin ligases. Seven in absentia homologue (SIAH) 2 is a host protein that can mediate the ubiquitination of proteins and is known for its interaction with NS5. In this study, comprehensive computational analysis was performed to characterize the protein-protein interactions between NS5, SIAH2, and STAT2 to gain insight into the residues and sites of interaction between these proteins. The objective of the study was to structurally characterize the NS5-STAT2, SIAH2-STAT2, and NS5-SIAH2 interactions along with the determination of the possible reaction pattern for the degradation of STAT2. Docking and physicochemical studies indicated that DENV NS5 may first interact with the host SIAH2, which can then proceed towards binding with STAT2 from the side of SIAH2. These implications are reported for the first time and require validation by wet-lab studies.

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Human TLR3 recognizes dengue virus and modulates viral replicationin vitro

Cited by 174 publications

References 49 publications

CLEC5A is critical for dengue virus–induced inflammasome activation in human macrophages

CLEC5A is critical for dengue virus–induced inflammasome activation in human macrophages

Characterization of the termini of the West Nile virus genome and their interactions with the small isoform of the 2′ 5′-oligoadenylate synthetase family

Structural modeling and analysis of dengue-mediated inhibition of interferon signaling pathway

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