Duck enteritis virus pUL47, as a late structural protein localized in the nucleus, mainly depends on residues 40 to 50 and 768 to 777 and inhibits IFN-β signalling by interacting with STAT1

He, Tianqiong; Wang, Mingshu; Cheng, Anchun; Yang, Qiao; Jia, Renyong; Wu, Ying; Huang, Juan; Chen, Shun; Zhao, Xinxin; Liu, Mafeng; Zhu, Dekang; Zhang, Shaqiu; Ou, Xuming; Mao, Sai; Gao, Qun; Sun, Di; Wen, Xinjian; Tian, Bin; Liu, Yunya; Yu, Yanling; Zhang, Ling; Pan, Leichang; Chen, Xiaoyue

doi:10.1186/s13567-020-00859-w

Cited by 12 publications

(10 citation statements)

References 70 publications

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“…Our previous work has reported that DPV UL47 is mainly localized in the nucleus at the early stage of infection and diffused in the cytoplasm at the late stage of infection (He et al, 2020). To investigate the effects of US3 protein on UL47 localization in DPV infection, DEF cells were infected with CHv and US3 and the subcellular localization of UL47 was detected at 6 h post-infection (hpi) and 10 hpi.…”

Section: Us3 Promotes the Cytoplasmic Translocation Of Ul47 In Duck P...mentioning

confidence: 99%

“…Currently, a lot of work on DPV research has been completed in our laboratory ( Xin et al, 2009 ; Wu et al, 2012a , b ; He et al, 2020 ). It has been reported that the DPV US3 protein is essential for virus replication, and US3 deletion significantly reduced viral titer and the efficiency of infectious virion formation during DPV replication ( Deng et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

“…Using these NLS signals, DPV UL47 protein translocated UL41 to the nuclei in the absence of other viral proteins. Moreover, DPV UL47 also inhibited IFNβ production and downregulated antiviral gene ISG expression ( He et al, 2018 , 2020 ).…”

Section: Introductionmentioning

confidence: 99%

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Duck plague virus US3 protein kinase phosphorylates UL47 and regulates the subcellular localization of UL47

Deng

Wan²,

Cheng³

et al. 2022

Front. Microbiol.

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Duck plague virus (DPV) belongs to the alphaherpesvirinae and causes high morbidity and mortality in waterfowl. UL47 is a large abundant structural protein in DPV, which means that UL47 protein plays an important role in virus replication. US3 protein, as a viral protein kinase in alphaherpesviruses, has been reported to be critical for DPV virion assembly. In this study, we over-expressed UL47 and US3 proteins and found that DPV UL47 protein was a phosphorylated substrate of US3 protein, which interacted and co-localized with US3 protein in the cytoplasm. US3-regulated phosphorylation of UL47 was important for the cytoplasmic localization of UL47 because non-phosphorylated UL47 was localized in the nucleus. The six sites of UL47 at Thr29, Ser30, Ser42, Thr47, Ser161, and Thr775 were identified as the phosphorylation targets of US3 protein. In vivo, UL47 phosphorylation was also detected but not in ΔUS3-infected cells. US3 protein promoted the cytoplasmic localization of UL47 at the late stage of infection, and the lack of US3 protein caused a delay in UL47 translocation to the cytoplasm. These results enhance our understanding of the functions of US3 during DPV infection and provide some references for DPV assembly.

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Section: Us3 Promotes the Cytoplasmic Translocation Of Ul47 In Duck P...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Duck plague virus US3 protein kinase phosphorylates UL47 and regulates the subcellular localization of UL47

Deng

Wan²,

Cheng³

et al. 2022

Front. Microbiol.

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“…UL47 was found to be the most abundant tegument protein, present at ≥1250 copies per virion [ 18 ]. Similarly, UL47 has been identified as a component protein of extracellular virions [ 19 ]. Both gB and UL47 proteins are abundant antigens in mature virions and virus infected cell plasma membranes [ 20 ].…”

Section: Discussionmentioning

confidence: 99%

Development of a Colloidal Gold Immunochromatographic Assay for Duck Enteritis Virus Detection Using Monoclonal Antibodies

et al. 2021

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Duck viral enteritis is a highly contagious and fatal disease of commercial waterfowl flocks. The disease occurs sporadically or epizootically in mainland China due to insufficient vaccinations. Early and rapid diagnosis is important for preventive intervention and the control of epizootic events in clinical settings. In this study, we generated two monoclonal antibodies (MAbs) that specifically recognized the duck enteritis virus (DEV) envelope glycoprotein B and tegument protein UL47, respectively. Using these MAbs, a colloidal gold-based immunochromatographic assay (ICA) was developed for the efficient detection of DEV antigens within 15 min. Our results showed that the detection limit of the developed ICA strip was 2.52 × 103 TCID50/mL for the virus infected cell culture suspension with no cross-reactivity with other pathogenic viruses commonly encountered in commercially raised waterfowl. Using samples from experimentally infected ducks, we demonstrated that the ICA detected the virus in cloacal swab samples on day three post-infection, demonstrating an 80% concordance with the PCR. For tissue homogenates from ducks succumbing to infection, the detection sensitivity was 100%. The efficient and specific detection by this ICA test provides a valuable, convenient, easy to use and rapid diagnostic tool for DVE under both laboratory and field conditions.

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“…In addition, DPV is immunosuppressive and exhibits broad cell tropism [ 39 , 40 ]. While knowledge on the molecular mechanism of DPV immune evasion is limited, the UL47 protein is known to interact with signal transducer and activator of transcription 1 (STAT1) to inhibit duck IFN-β production [ 41 ]. In this study, we found that the DPV UL41 protein abrogated RIG-I/MDA5-mediated duck IFN-β production by downregulating the mRNA levels of important adaptors, and the conserved sites of the UL41 protein, E229, D231, and D232, were responsible for this activity.…”

Section: Introductionmentioning

confidence: 99%

Duck plague virus UL41 protein inhibits RIG-I/MDA5-mediated duck IFN-β production via mRNA degradation activity

Wang

Cheng

et al. 2022

Vet Res

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Retinoic acid-inducible gene I (RIG-I)-like receptors (RLRs) are cytosolic pattern recognition receptors that initiate innate antiviral immunity. Recent reports found that duck RLRs significantly restrict duck plague virus (DPV) infection. However, the molecular mechanism by which DPV evades immune responses is unknown. In this study, we first found that the DPV UL41 protein inhibited duck interferon-β (IFN-β) production mediated by RIG-I and melanoma differentiation-associated gene 5 (MDA5) by broadly downregulating the mRNA levels of important adaptor molecules, such as RIG-I, MDA5, mitochondrial antiviral signalling protein (MAVS), stimulator of interferon gene (STING), TANK-binding kinase 1 (TBK1), and interferon regulatory factor (IRF) 7. The conserved sites of the UL41 protein, E229, D231, and D232, were responsible for this activity. Furthermore, the DPV CHv-BAC-ΔUL41 mutant virus induced more duck IFN-β and IFN-stimulated genes (Mx, OASL) production in duck embryo fibroblasts (DEFs) than DPV CHv-BAC parent virus. Our findings provide insights into the molecular mechanism underlying DPV immune evasion.

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Duck enteritis virus pUL47, as a late structural protein localized in the nucleus, mainly depends on residues 40 to 50 and 768 to 777 and inhibits IFN-β signalling by interacting with STAT1

Cited by 12 publications

References 70 publications

Duck plague virus US3 protein kinase phosphorylates UL47 and regulates the subcellular localization of UL47

Duck plague virus US3 protein kinase phosphorylates UL47 and regulates the subcellular localization of UL47

Development of a Colloidal Gold Immunochromatographic Assay for Duck Enteritis Virus Detection Using Monoclonal Antibodies

Duck plague virus UL41 protein inhibits RIG-I/MDA5-mediated duck IFN-β production via mRNA degradation activity

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