scholarly journals Infectious Bursal Disease Virus VP3 Upregulates VP1-Mediated RNA-Dependent RNA Replication

2015 ◽  
Vol 89 (21) ◽  
pp. 11165-11168 ◽  
Author(s):  
Diego Ferrero ◽  
Damià Garriga ◽  
Aitor Navarro ◽  
José F. Rodríguez ◽  
Núria Verdaguer
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Rna Replication ◽  
Life Cycles ◽  
Infectious Bursal Disease ◽  
Untranslated Regions ◽  
Genome Replication ◽  
Ribonucleoprotein Complexes ◽  
Bursal Disease

Genome replication is a critical step in virus life cycles. Here, we analyzed the role of the infectious bursal disease virus (IBDV) VP3, a major component of IBDV ribonucleoprotein complexes, on the regulation of VP1, the virus-encoded RNA-dependent RNA polymerase (RdRp). Data show that VP3, as well as a peptide mimicking its C-terminal domain, efficiently stimulates the ability of VP1 to replicate synthetic single-stranded RNA templates containing the 3′ untranslated regions (UTRs) from the IBDV genome segments.

scholarly journals Voltage-Dependent Anion Channel 1 Interacts with Ribonucleoprotein Complexes To Enhance Infectious Bursal Disease Virus Polymerase Activity

2017 ◽  
Vol 91 (16) ◽  
Author(s):  
Chunyan Han ◽  
Xiangwei Zeng ◽  
Shuai Yao ◽  
Li Gao ◽  
Lizhou Zhang ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Viral Proteins ◽  
Polymerase Activity ◽  
Infectious Bursal Disease ◽  
Cellular Factor ◽  
Ribonucleoprotein Complexes ◽  
Viral Yield ◽  
Bursal Disease

ABSTRACTInfectious bursal disease virus (IBDV) is a double-stranded RNA (dsRNA) virus. Segment A contains two overlapping open reading frames (ORFs), which encode viral proteins VP2, VP3, VP4, and VP5. Segment B contains one ORF and encodes the viral RNA-dependent RNA polymerase, VP1. IBDV ribonucleoprotein complexes are composed of VP1, VP3, and dsRNA and play a critical role in mediating viral replication and transcription during the virus life cycle. In the present study, we identified a cellular factor, VDAC1, which was upregulated during IBDV infection and found to mediate IBDV polymerase activity. VDAC1 senses IBDV infection by interacting with viral proteins VP1 and VP3. This association is caused by RNA bridging, and all three proteins colocalize in the cytoplasm. Furthermore, small interfering RNA (siRNA)-mediated downregulation ofVDAC1resulted in a reduction in viral polymerase activity and a subsequent decrease in viral yield. Moreover, overexpression of VDAC1 enhanced IBDV polymerase activity. We also found that the viral protein VP3 can replace segment A to execute polymerase activity. A previous study showed that mutations in the C terminus of VP3 directly influence the formation of VP1-VP3 complexes. Our immunoprecipitation experiments demonstrated that protein-protein interactions between VDAC1 and VP3 and between VDAC1 and VP1 play a role in stabilizing the interaction between VP3 and VP1, further promoting IBDV polymerase activity.IMPORTANCEThe cellular factor VDAC1 controls the entry and exit of mitochondrial metabolites and plays a pivotal role during intrinsic apoptosis by mediating the release of many apoptogenic molecules. Here we identify a novel role of VDAC1, showing that VDAC1 interacts with IBDV ribonucleoproteins (RNPs) and facilitates IBDV replication by enhancing IBDV polymerase activity through its ability to stabilize interactions in RNP complexes. To our knowledge, this is the first report that VDAC1 is specifically involved in regulating IBDV RNA polymerase activity, providing novel insight into virus-host interactions.

scholarly journals Potential reverse spillover of infectious bursal disease virus at the interface of commercial poultry and wild birds

Virus Genes ◽  
2020 ◽  
Vol 56 (6) ◽  
pp. 705-711
Author(s):  
Rania F. El Naggar ◽  
Mohammed A. Rohaim ◽  
Muhammad Munir
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Potential Role ◽  
Wild Birds ◽  
Infectious Bursal Disease ◽  
Free Living ◽  
Bean Goose ◽  
Bursal Disease ◽  
Commercial Poultry

AbstractRecently, multiple spillover events between domesticated poultry and wild birds have been reported for several avian viruses. This phenomenon highlights the importance of the livestock-wildlife interface in the possible emergence of novel viruses. The aim of the current study was to investigate the potential spillover and epidemiological links of infectious bursal disease virus (IBDV) between wild birds and domestic poultry. To this end, twenty-eight cloacal swabs were collected from four species of free-living Egyptian wild birds (i.e. mallard duck, bean goose, white-fronted goose and black-billed magpie). Genetic and phylogenetic analysis of three positive isolates revealed that the IBDV/USC-1/2019 strain clustered with previously reported very virulent IBDV (vvIBDV) Egyptian isolates. Interestingly, two other wild bird-origin isolates (i.e. IBDV/USC-2/2019 and IBDV/USC-3/2019) grouped with a vaccine strain that is being used in commercial poultry. In conclusion, our results revealed the molecular detection of vaccine and vvIBDV-like strains in Egyptian wild birds and highlighted the potential role of wild birds in IBDV epidemiology in disease-endemic regions.

scholarly journals Identification of Chicken CD74 as a Novel Cellular Attachment Receptor for Infectious Bursal Disease Virus in Bursa B Lymphocytes

2019 ◽  
Vol 94 (2) ◽  
Author(s):  
Aijing Liu ◽  
Qing Pan ◽  
Yue Li ◽  
Nana Yan ◽  
Jing Wang ◽  
...  
Keyword(s):  
B Cells ◽  
Cell Line ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
B Lymphocyte ◽  
Pivotal Role ◽  
Infectious Bursal Disease ◽  
Antigenic Peptides ◽  
Bursal Disease

ABSTRACT Infectious bursal disease virus (IBDV) is an important member of the Birnaviridae family, causing severe immunosuppressive disease in chickens. The major capsid protein VP2 is responsible for the binding of IBDV to the host cell and its cellular tropism. In order to find proteins that potentially interact with IBDV VP2, a liquid chromatography-mass spectrometry (LC-MS) assay was conducted, and the host chicken CD74 protein was identified. Here, we investigate the role of chicken CD74 in IBDV attachment. Coimmunoprecipitation assays indicated that the extracellular domain of CD74 interacted with the VP2 proteins of multiple IBDV strains. Knockdown and overexpression experiments showed that CD74 promotes viral infectivity. Confocal assays showed that CD74 overexpression allows the attachment of IBDV and subvirus-like particles (SVPs) to the cell surface of nonpermissive cells, and quantitative PCR (qPCR) analysis further confirmed the attachment function of CD74. Anti-CD74 antibody, soluble CD74, depletion of CD74 by small interfering RNA (siRNA), and CD74 knockdown in the IBDV-susceptible DT40 cell line significantly inhibited IBDV binding, suggesting a pivotal role of this protein in virus attachment. These findings demonstrate that CD74 is a novel important receptor for IBDV attachment to the chicken B lymphocyte cell line DT40. IMPORTANCE CD74 plays a pivotal role in the correct folding and functional stability of major histocompatibility complex class II (MHC-II) molecules and in the presentation of antigenic peptides, acting as a regulatory factor in the antigen presentation process. In our study, we demonstrate a novel role of CD74 during IBDV infection, showing that chicken CD74 plays a significant role in IBDV binding to target B cells by interacting with the viral VP2 protein. This is the first report demonstrating that CD74 is involved as a novel attachment receptor in the IBDV life cycle in target B cells, thus contributing new insight into host-pathogen interactions.

scholarly journals Infectious Bursal Disease Virus: Ribonucleoprotein Complexes of a Double-Stranded RNA Virus

2009 ◽  
Vol 386 (3) ◽  
pp. 891-901 ◽  
Author(s):  
Daniel Luque ◽  
Irene Saugar ◽  
María Teresa Rejas ◽  
José L. Carrascosa ◽  
José F. Rodríguez ◽  
...  
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Rna Virus ◽  
Infectious Bursal Disease ◽  
Double Stranded Rna ◽  
Ribonucleoprotein Complexes ◽  
Bursal Disease

scholarly journals MicroRNA gga-miR-130b Suppresses Infectious Bursal Disease Virus Replication via Targeting of the Viral Genome and Cellular Suppressors of Cytokine Signaling 5

2017 ◽  
Vol 92 (1) ◽  
Author(s):  
Mengjiao Fu ◽  
Bin Wang ◽  
Xiang Chen ◽  
Zhiyuan He ◽  
Yongqiang Wang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Viral Genome ◽  
Infectious Bursal Disease Virus ◽  
Host Cells ◽  
Infectious Bursal Disease ◽  
Cytokine Signaling ◽  
Type I ◽  
Bursal Disease ◽  
Suppressors Of Cytokine Signaling

ABSTRACTMicroRNAs (miRNAs) are small noncoding RNAs that regulate gene expression posttranscriptionally through silencing or degrading their targets, thus playing important roles in the immune response. However, the role of miRNAs in the host response against infectious bursal disease virus (IBDV) infection is not clear. In this study, we show that the expression of a series of miRNAs was significantly altered in DF-1 cells after IBDV infection. We found that the miRNA gga-miR-130b inhibited IBDV replication via targeting the specific sequence of IBDV segment A and enhanced the expression of beta interferon (IFN-β) by targeting suppressors of cytokine signaling 5 (SOCS5) in host cells. These findings indicate that gga-miR-130b-3p plays a crucial role in host defense against IBDV infection.IMPORTANCEThis work shows that gga-miR-130b suppresses IBDV replication via directly targeting the viral genome and cellular SOCS5, the negative regulator for type I interferon expression, revealing the mechanism underlying gga-miR-130-induced inhibition of IBDV replication. This information will be helpful for the understanding of how host cells combat pathogenic infection by self-encoded small RNA and furthers our knowledge of the role of microRNAs in the cell response to viral infection.

Modelling the interaction between Infectious Bursal Disease Virus VP3 polypeptide and dsRNA: identification of key residues for ribonucleoprotein assembly and virus replication

2020 ◽  
Author(s):  
Idoia Busnadiego ◽  
Maria T Martín ◽  
Diego S Ferrero ◽  
María G Millán de la Blanca ◽  
Laura Broto ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Infectious Bursal Disease Virus ◽  
Interaction Model ◽  
Infectious Bursal Disease ◽  
Surface Plasmon Resonance Analysis ◽  
Ribonucleoprotein Complexes ◽  
Binding Function ◽  
Dsrna Binding ◽  
Bursal Disease

ABSTRACTThe interaction of the structural VP3 polypeptide of infectious bursal disease virus (IBDV) with virus-encoded dsRNA is essential both for the assembly of ribonucleoprotein complexes responsible for genome transcription and replication and for the evasion of host’s antiviral responses. Surface plasmon resonance analysis allowed us to determine the kinetic constants of the VP3-dsRNA interaction as well as to map the VP3 dsRNA bipartite dsRNA binding domain (dsRBD), uncovering the specific role of the previously described Patch1 and Patch2 dsRB subdomains. Here we show that the Patch1 domain plays a primary binding function while Patch2 exerts a subordinate role stabilizing VP3-dsRNA complexes. The use of a set of VP3 mutant versions facilitated the identification of K99 and K106 within Patch1 as the essential residues for the formation of VP3-dsRNA complexes. Furthermore, replacement of either one of these two residues by aspartic acid completely thwarts both evasion from host’s sensors and virus replication. Data presented here allow us to propose a VP3-dsRNA interaction model that should help to further elucidate the mechanics of IBDV morphogenesis and genome packaging as well as to better understand how VP3 counteracts recognition of virus-encoded dsRNA by specialized host’s sensors.

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