Characterization of duck enteritis virus UL53 gene and glycoprotein K

Zhang, Shunchuan; Xiang, Jun; Cheng, Anchun; Wang, Mingshu; Wu, Ying; Yang, Xiaoyuan; Zhu, Dekang; Jia, Renyong; Luo, Qihui; Chen, Zhengli; Chen, Xiaoyue

doi:10.1186/1743-422x-8-235

Cited by 18 publications

(14 citation statements)

References 36 publications

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“…To identify the DEV UL41 gene type, we studied its transcription and expression kinetics at different time points post-infection using RT-qPCR and western blot analysis, respectively. Based on previous studies [ 32 , 37 , 48 , 49 ], we suggested that accumulation of the DEV pUL41 may occur during the late stage of infection. IE genes are expressed in the presence of CHX, a protein synthesis inhibitor, while transcription of E and L genes is suppressed in the presence of CHX [ 50 ].…”

Section: Discussionmentioning

confidence: 84%

Molecular characterization of duck enteritis virus UL41 protein

Wang

Cao

et al. 2018

Virol J

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BackgroundDuck enteritis virus (DEV) belongs to the subfamily Alphaherpesvirinae, and information on the DEV UL41 gene is limited.MethodsThe DEV UL41 gene was cloned into the pET32a(+) vector and expressed in a prokaryotic expression system. Antiserum was raised against a bacterially expressed UL41-His fusion protein for further experiments. Transcription was quantified and UL41 protein expression levels were determined in DEV-infected cells at different time points by RT-qPCR and western blotting, respectively. DEV virions were purified by sucrose gradient centrifugation and analyzed by mass spectrometry to identify protein content. We confirmed the DEV UL41 gene kinetic class using a pharmacological test. IFA was used to analyze the intracellular localization of pUL41.ResultsThe recombinant expression plasmid, pET-32a(+)-UL41, which highly expresses a 76.0 kDa fusion protein, was constructed and expressed in E. coli BL21 (DE3) after induction with 0.2 mM IPTG at 30 °C for 10 h, generating a specific mouse anti-UL41 protein polyclonal antibody. RT-qPCR and western blot analyses revealed that the UL41 transcript number peaked at 36 hpi, and peak protein expression occurred at 48 hpi. The pharmacological test showed that UL41 was a γ2 gene. Mass spectrometry analysis showed that pUL41 was a virion component. IFA results revealed that pUL41 was localized throughout DEV-infected cells but only localized to the cytoplasm of transfected cells. DEV pUL47 translocated pUL41 to the nuclei of DEF cells; this translocation was dependent on predicted pUL47 NLS signals (40–50 aa and 768–777 aa).ConclusionsDEV UL41 is a γ2 gene that encodes a virion structural protein, pUL41 localizes throughout DEV-infected cells but only localizes to the cytoplasm of transfected cells. pUL41 cannot autonomously localize to the nucleus, as this nuclear localization is dependent on predicted DEV pUL47 NLS signals (40–50 aa and 768–777 aa).

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Section: Discussionmentioning

confidence: 84%

Molecular characterization of duck enteritis virus UL41 protein

Wang

Cao

et al. 2018

Virol J

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“…Indeed, generation of MP may be closely associated with the initiation of apoptosis and necrosis (Ardoin et al, 2007). Whether stress-inducible proteins, such as hypoxia-inducible factor 1α (HIF-1α), heat-shock factor (HSF-1), heat-shock protein (Hsp) family, nuclear factor κB (NF-κB), Jun NH2-terminal kinase (JNK), and p53 (Ohiro et al, 2003; Razorenova et al, 2005; Thompson and Locarnini, 2007; Zinkernagel et al, 2007; De Maio, 2011; Li et al, 2011; Rawat and Mitra, 2011; Zhang et al, 2011) and MHC class I polypeptide-related sequence A and B (MICA, MICB; Stern-Ginossar and Mandelboim, 2009) are involved, remains to be determined. Nevertheless, a broad array of pro-inflammatory cytokines, such as tumor necrosis factor (TNF), interleukin-1 (IL-1), IL-6, and type 1 interferons (IFN-I) are produced in response to infection (Medzhitov and Horng, 2009), and many of these induce MP shedding in the absence of infection (Combes et al, 1999; Sheremata et al, 2006; Penet et al, 2008).…”

Section: Mp In Inflammatory Conditionsmentioning

confidence: 99%

Microparticles as Immune Regulators in Infectious Disease ? An Opinion

Ling¹,

Combes²,

Grau³

et al. 2011

Front. Immun.

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Despite their clear relationship to immunology, few existing studies have examined the potential role of microparticles (MP) in infectious disease. MP have a different size range from exosomes and apoptotic bodies, with which they are often grouped and arise by different mechanisms in association with inflammatory cytokine action or stress on the source cell. Infection with pathogens usually leads to the expression of a range of inflammatory cytokines and chemokines, as well as significant stress in both infected and uninfected cells. It is thus reasonable to infer that infection-associated inflammation also leads to MP production. MP are produced by most of the major cell types in the immune system, and appear to be involved at both innate and adaptive levels, potentially serving different functions in each. Thus, they do not appear to have a universal function; instead their functions are source- or stimulus-dependent, although likely to be primarily either pro- or anti-inflammatory. We argue that in infectious diseases, MP may be able to deliver antigen, derived from the biological cargo acquired from their cells of origin, to antigen-presenting cells. Another potential benefit of MP would be to transfer and/or disseminate phenotype and function to target cells. However, MP may also potentially be manipulated, particularly by intracellular pathogens, for survival advantage.

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“…The characteristics of some genes from DEV had been reported [45][46][47][48][49][50][51][52][53][54][55][56][57][58][59][60][61][62][63][64]. However, the function of VP16 of duck enteritis virus encoded by the UL48 gene was hardly studied.…”

Section: Introductionmentioning

confidence: 99%

Duck Enteritis Virus VP16 Antagonizes IFN-β-Mediated Antiviral Innate Immunity

Wang

Cheng

et al. 2020

Journal of Immunology Research

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Duck enteritis virus (DEV) can successfully evade the host innate immune responses and establish a lifelong latent infection in the infected host. However, the study about how DEV escapes host innate immunity is still deficient up to now. In this study, for the first time, we identified a viral protein VP16 by which DEV can obviously downregulate the production of IFN-β in duck embryo fibroblast (DEF). Our results showed that ectopic expression of VP16 decreased duck IFN-β (duIFN-β) promoter activation and significantly inhibited the mRNA transcription of IFN-β. Further study showed that VP16 can also obviously inhibit the mRNA transcription of interferon-stimulated genes (ISGs), such as myxovirus resistance protein (Mx) and interferon-induced oligoadenylate synthetase-like (OASL). Furthermore, we found that this anti-interferon activity of VP16 depended on its N-terminus (aa1-200). Coexpression analysis revealed that VP16 selectively blocked duIFN-β promoter activity at the duIRF7 level rather than duIRF1. Based on the results of coimmunoprecipitation analysis (co-IP) and indirect immunofluorescence assay (IFA), VP16 was able to bind to duck IRF7 (duIRF7) directly, but did not interact with duck IRF1 (duIRF1) in vitro.

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Characterization of duck enteritis virus UL53 gene and glycoprotein K

Cited by 18 publications

References 36 publications

Molecular characterization of duck enteritis virus UL41 protein

Molecular characterization of duck enteritis virus UL41 protein

Microparticles as Immune Regulators in Infectious Disease ? An Opinion

Duck Enteritis Virus VP16 Antagonizes IFN-β-Mediated Antiviral Innate Immunity

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