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  • Qi, Xiaole  (24)
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  • 1
    Language: English
    In: 2014, Vol.9(12), p.e115422
    Description: Avian leukosis virus subgroup J (ALV-J) has induced serious clinical outbreaks and has become a serious infectious disease of chickens in China. We describe here the creation of a recombinant ALV-J tagged with the enhanced green fluorescent protein (named rHPRS-103EGFP). We successfully utilize the rHPRS-103EGFP to visualize viral infection and for development of a simplified serum-neutralization test.
    Keywords: Research Article ; Biology And Life Sciences
    E-ISSN: 1932-6203
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  • 2
    Language: English
    In: PLoS ONE, Dec 18, 2014, Vol.9(12)
    Description: Avian leukosis virus subgroup J (ALV-J) has induced serious clinical outbreaks and has become a serious infectious disease of chickens in China. We describe here the creation of a recombinant ALV-J tagged with the enhanced green fluorescent protein (named rHPRS-103EGFP). We successfully utilize the rHPRS-103EGFP to visualize viral infection and for development of a simplified serum-neutralization test.
    Keywords: Antibodies – Health Aspects ; Fluorescence – Health Aspects
    ISSN: 1932-6203
    Source: Cengage Learning, Inc.
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  • 3
    In: PLoS ONE, 2013, Vol.8(7)
    Description: Infectious bursal disease virus (IBDV) is a pathogen of worldwide significance to the poultry industry. Although the P DE and P FG domains of the capsid protein VP2 contribute significantly to virulence and fitness, the detailed molecular basis for the pathogenicity of IBDV is still not fully understood. Because residues 253 and 284 of VP2 are not the sole determinants of virulence, we hypothesized that other residues involved in virulence and fitness might exist in the P DE and P FG domains of VP2. To test this, five amino acid changes selected by sequence comparison of the P DE and P FG domains of VP2 were introduced individually using a reverse genetics system into the virulent strain (rGx-F9VP2). Then reverse mutations of the selected residues 249 and 256 were introduced individually into the attenuated strain (rGt). Seven modified viruses were generated and evaluated in vitro (CEF cells) and in vivo (SPF chicken). For residue 249, Q249R could elevate in vitro and reduce in vivo the replication of rGx-F9VP2 while R249Q could reduce in vitro and elevate in vivo the replication of rGt; meanwhile Q249R reduced the virulence of rGx-F9VP2 while R249Q increased the virulence of rGt, which indicated that residue 249 significantly contributed to the replication and virulence of IBDV. For residue 256, I256V could elevate in vitro and reduce in vivo the replication of rGx-F9VP2 while V256I could reduce in vitro but didn’t change in vivo the replication of rGt; although V256I didn’t increase the virulence of rGt, I256V obviously reduced the virulence of virulent IBDV. The present results demonstrate for the first time, to different extent, residues 249 and 256 of VP2 are involved in the replication efficiency and virulence of IBDV; this is not only beneficial to further understanding of pathogenic mechanism but also to the design of newly tailored vaccines against IBDV.
    Keywords: Research Article ; Biology ; Veterinary Science
    E-ISSN: 1932-6203
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  • 4
    Language: English
    In: Virus Research, 02 December 2015, Vol.210, pp.232-240
    Description: Infectious bursal disease virus (IBDV) causes a highly contagious disease in young chickens and leads to significant economic loss in the poultry industry. The identification of host cellular molecules that bind to IBDV will improve the understanding of the underlying pathogenic mechanisms. In this study, using a virus overlay protein-binding assay (VOPBA) and mass spectrometry (MS) analysis, IBDV was found to bind chicken Anx2, a membrane protein fraction from DF-1 cells. Its interactions were further confirmed by an overlay assay. The results of an immunofluorescence assay and flow cytometry showed that Anx2 could be expressed and colocalized with IBDV on the surface of infected cells. Moreover, either the soluble recombinant Anx2 or an anti-Anx2 antibody could inhibit IBDV binding to and infection of DF-1 cells in a dose-dependent manner. The knockdown of Anx2 of DF-1 cells by small interfering RNA clearly reduced the subsequent virus yield, and overexpression of Anx2 was capable of enhancing the virus yield. These results indicate, for the first time, that binding to Anx2 is beneficial for IBDV infection.
    Keywords: Chicken Anx2 ; Ibdv ; Binding ; Virus Infection ; Biology
    ISSN: 0168-1702
    E-ISSN: 1872-7492
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  • 5
    Language: English
    In: Archives of Virology, 2015, Vol.160(10), pp.2445-2453
    Description: The entry of enveloped viruses into host cells requires the fusion of viral and cell membranes. These membrane fusion reactions are mediated by virus-encoded glycoproteins. In the case of avian metapneumovirus (aMPV), the fusion (F) protein alone can mediate virus entry and induce syncytium formation in vitro . To investigate the fusogenic activity of the aMPV F protein, we compared the fusogenic activities of three subtypes of aMPV F proteins using a TCSD 50 assay developed in this study. Interestingly, we found that the F protein of aMPV subtype B (aMPV/B) strain VCO3/60616 (aMPV/vB) was hyperfusogenic when compared with F proteins of aMPV/B strain aMPV/f (aMPV/fB), aMPV subtype A (aMPV/A), and aMPV subtype C (aMPV/C). We then further demonstrated that the amino acid (aa) residue 149F contributed to the hyperfusogenic activity of the aMPV/vB F protein. Moreover, we revealed that residue 149F had no effect on the fusogenic activities of aMPV/A, aMPV/C, and human metapneumovirus (hMPV) F proteins. Collectively, we provide the first evidence that the amino acid at position 149 affects the fusogenic activity of the aMPV/B F protein, and our findings will provide new insights into the fusogenic mechanism of this protein.
    Keywords: Amino Acids ; Glycoproteins ; Zoonoses;
    ISSN: 0304-8608
    E-ISSN: 1432-8798
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  • 6
    Language: English
    In: Virology, December 2017, Vol.512, pp.211-221
    Description: Infectious bursal disease virus (IBDV) is an important immunosuppressive virus of chickens. Although the gene functions of IBDV have been well characterized, the host responses during IBDV infection remain much poor. In the present study, casein kinase 1 alpha (CK1α), a novel VP2-associated protein, was down-regulated during IBDV replication in DF1 cells. Further experiments showed that siRNA-mediated knockdown of CK1α inhibited IBDV replication, while overexpression of CK1α promoted IBDV growth. Finally, we revealed that the effects of CK1α expression level on IBDV replication were involved in the negative regulation of CK1α on type I interferon receptor (IFNAR1), because ubiquitination assay analyses demonstrated that CK1α could promote the ubiquitination of IFNAR1, thereby affecting the stability of this receptor. In conclusion, down-regulation of CK1α during IBDV infection as a host defense response increased abundance of IFNAR1, which in turn enhanced an inhibitory effect on IBDV replication.
    Keywords: Ibdv ; Vp2 ; Ck1α ; Ifnar1 ; Host Defense ; Viral Replication ; Biology
    ISSN: 0042-6822
    E-ISSN: 1096-0341
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  • 7
    In: Scientific Reports, 2017, Vol.7
    Description: Avian gyrovirus 2 (AGV2) was the second member of the viral genus Cyclovirus to be discovered. This virus poses a significant potential threat to humans and poultry due to its global dissemination and infectiousness. We used three overlapping polymerase chain reactions (PCRs) to map the whole genome of AGV2. We then modelled the evolutionary history of these novel sequence data in the context of related sequences from GenBank. We analysed the viral protein characteristics of the different phylogenetic groups and explored differences in evolutionary trends between Chinese strains and strains from other countries. We obtained 17 avian-sourced AGV2 whole genomes from different regions of China from 2015 to 2016. Phylogenetic analyses of these Chinese AGV2 sequences and related sequences produced four distinct groups (A-D) with significant bootstrap values. We also built phylogenies using predicted viral protein sequences. We found a potential hypervariable region in VP1 at sites 288-314, and we identified the amino acid changes responsible for the distinct VP2 and VP3 groups. Three new motifs in the AGV2 5'-UTR direct repeat (DR) region were discovered and grouped. The novel characteristics and diverse research on the AGV2 genome provide a valuable framework for additional research.
    Keywords: Biology;
    E-ISSN: 2045-2322
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  • 8
    Language: English
    In: Virus Research, 04 May 2015, Vol.203, pp.92-95
    Description: Infectious bursal disease virus (IBDV) is a bi-segmented, double-stranded RNA virus that belongs to the genus of the family of . The co-evolution of genome segments is a major evolutionary feature for IBDV. However, in recent years, some strains exhibited markedly different genetic relationships for segments A and B. In this study, we firstly isolated a new type of reassortment IBDV strain named IBD13HeB01 from northern China. The full-length genomes of segments A and B were cloned and identified. Sequence analysis revealed that IBD13HeB01 was a segment-reassortment strain, whose segment A was derived from very virulent strain and segment B from attenuated IBDV. In addition, the virulence of IBD13HeB01 strain was evaluated using SPF chickens. This study is not only beneficial for further understanding of the viral evolution but also suggests the potential risk of application of the live vaccines of IBDV.
    Keywords: Infectious Bursal Disease Virus (Ibdv) ; Reassortant ; Genome ; Evolution ; Biology
    ISSN: 0168-1702
    E-ISSN: 1872-7492
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  • 9
    Language: English
    In: Oncotarget, 06 December 2016, Vol.7(49), pp.80275-80287
    Description: Avian leukosis virus subgroup J (ALV-J) is an oncogenic virus causing hemangiomas and myeloid tumors in chickens. Interleukin-6 (IL-6) is a multifunctional pro-inflammatory interleukin involved in many types of cancer. We previously demonstrated that IL-6 expression was induced following ALV-J infection in chickens. The aim of this study is to characterize the mechanism by which ALV-J induces IL-6 expression, and the role of IL-6 in tumor development. Our results demonstrate that ALV-J infection increases IL-6 expression in chicken splenocytes, peripheral blood lymphocytes, and vascular endothelial cells. IL-6 production is induced by the ALV-J envelope protein gp85 and capsid protein p27 via PI3K- and NF-κB-mediated signaling. IL-6 in turn induced expression of vascular endothelial growth factor (VEGF)-A and its receptor, VEGFR-2, in vascular endothelial cells and embryonic vascular tissues. Suppression of IL-6 using siRNA inhibited the ALV-J induced VEGF-A and VEGFR-2 expression in vascular endothelial cells, indicating that the ALV-J-induced VEGF-A/VEGFR-2 expression is mediated by IL-6. As VEGF-A and VEGFR-2 are important factors in oncogenesis, our findings suggest that ALV-J hijacks IL-6 to promote tumorigenesis, and indicate that IL-6 could potentially serve as a therapeutic target in ALV-J infections.
    Keywords: Alv-J ; Immune Response ; Immunity ; Immunology and Microbiology Section ; Vegf-A ; Vegfr-2 ; Interleukin 6 ; Tumorigenesis ; Avian Leukosis -- Enzymology ; Avian Leukosis Virus -- Metabolism ; Endothelial Cells -- Enzymology ; Interleukin-6 -- Metabolism ; Nf-Kappa B -- Metabolism ; Phosphatidylinositol 3-Kinase -- Metabolism ; Spleen -- Enzymology ; Vascular Endothelial Growth Factor A -- Metabolism
    E-ISSN: 1949-2553
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  • 10
    Language: English
    In: Virus Research, 04 January 2016, Vol.211, pp.73-78
    Description: VP3 protein is a structural protein which plays important roles in the virus assembly and the inhibition of antiviral innate immunity of infectious bursal disease virus (IBDV). To explore the potential roles of VP3 in the interplay of IBDV with the host cell, an immunoprecipitation (IP)-coupled mass spectra (MS) screening was performed and the host cellular ribosomal protein L4 (RPL4) was identified as a putative interacting partner of VP3 protein. The interaction of RPL4 with VP3 was further confirmed by co-immunoprecipitation (co-IP) and their colocalization in DF1 cells were observed by confocal microscopy. In addition, knockdown of RPL4 in DF1 cells resulted in reductions of the viral protein pVP2 expression and the virus titers, which reveals a significant role of RPL4 in IBDV replication. Taken together, we indicated for the first time that ribosomal protein L4 (RPL4) was an interacting partner of VP3 and involved in the modulation of IBDV replication. The present study contributes to further understanding the pathogenic mechanism of IBDV.
    Keywords: Infectious Bursal Disease Virus ; Ribosomal Protein L4 ; Vp3 ; Interaction ; Replication ; Biology
    ISSN: 0168-1702
    E-ISSN: 1872-7492
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