scholarly journals Synthesis of Reassortant Infectious Bursal Disease Virus in Chickens Injected Directly with Infectious Clones from Different Virus Strains

2005 ◽  
Vol 37 (3) ◽  
pp. 192-198 ◽  
Author(s):  
Long Li ◽  
Yao-Wei Huang ◽  
Lian-Sheng Wang ◽  
Wang-Jun Wan ◽  
Lian Yu
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Field Isolate ◽  
Histopathological Change ◽  
Eukaryotic Expression ◽  
Infectious Bursal Disease ◽  
Structural Protein ◽  
Infectious Clones ◽  
Bursal Disease

Abstract The infectious bursal disease virus (IBDV), a member of the Birnaviridae family, containing a bisegmented double-stranded RNA genome, encodes four structural viral proteins, VP1, VP2, VP3, and VP4, as well as a non-structural protein, VP5. In the present paper, the segment A from two IBDV strains, field isolate ZJ2000 and attenuated strain HZ2, were inserted into one NaeI site by site-directed silent mutagenesis and subcloned into the eukaryotic expression plasmid pCI under the control of the human cytomegalovirus (hCMV) immediate early enhancer and promoter to construct the recombinant plasmids pCI-AKZJ2000 and pCI-AKHZ2, respectively. Each of the two recombinants was combined with another recombinant pCI plasmid containing the marked segment B of strain HZ2 (pCI-mB), and injected intramuscularly into nonimmunized chickens. Two chimeric IBDV strains were recovered from the chickens. Two out of eight chickens in each of two groups showed the bursal histopathological change. The reassortant virus derived from pCI-AKZJ2000/pCI-mB can infect chicken embryos and shows relatively low virulence. We have developed a novel virus reverse genetic approach for the study of IBDV. The results also form the basis for investigating the role of VP1 in viral replication and pathogenecity.

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 Capsid Assembly and Maturation by Structural Rearrangements of a Transient Molecular Switch

2007 ◽  
Vol 81 (13) ◽  
pp. 6869-6878 ◽  
Author(s):  
Daniel Luque ◽  
Irene Saugar ◽  
José F. Rodríguez ◽  
Nuria Verdaguer ◽  
Damiá Garriga ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Scaffolding Protein ◽  
Infectious Bursal Disease ◽  
Capsid Assembly ◽  
Protein Oligomerization ◽  
Structural Protein ◽  
Bursal Disease ◽  
Α Helix

ABSTRACT Infectious bursal disease virus (IBDV), a double-stranded RNA (dsRNA) virus belonging to the Birnaviridae family, is an economically important avian pathogen. The IBDV capsid is based on a single-shelled T=13 lattice, and the only structural subunits are VP2 trimers. During capsid assembly, VP2 is synthesized as a protein precursor, called pVP2, whose 71-residue C-terminal end is proteolytically processed. The conformational flexibility of pVP2 is due to an amphipathic α-helix located at its C-terminal end. VP3, the other IBDV major structural protein that accomplishes numerous roles during the viral cycle, acts as a scaffolding protein required for assembly control. Here we address the molecular mechanism that defines the multimeric state of the capsid protein as hexamers or pentamers. We used a combination of three-dimensional cryo-electron microscopy maps at or close to subnanometer resolution with atomic models. Our studies suggest that the key polypeptide element, the C-terminal amphipathic α-helix, which acts as a transient conformational switch, is bound to the flexible VP2 C-terminal end. In addition, capsid protein oligomerization is also controlled by the progressive trimming of its C-terminal domain. The coordination of these molecular events correlates viral capsid assembly with different conformations of the amphipathic α-helix in the precursor capsid, as a five-α-helix bundle at the pentamers or an open star-like conformation at the hexamers. These results, reminiscent of the assembly pathway of positive single-stranded RNA viruses, such as nodavirus and tetravirus, add new insights into the evolutionary relationships of dsRNA viruses.

scholarly journals The expression in plants of an engineered VP2 protein of Infectious Bursal Disease Virus induces formation of structurally heterogeneous particles that protect from a very virulent viral strain

PLoS ONE ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. e0247134
Author(s):  
Carla Marusic ◽  
Charifa Drissi Touzani ◽  
Alessio Bortolami ◽  
Marcello Donini ◽  
Claudia Zanardello ◽  
...  
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Neutralizing Antibodies ◽  
Sucrose Density Gradient ◽  
Bursa Of Fabricius ◽  
Infectious Bursal Disease ◽  
Structural Protein ◽  
Vp2 Protein ◽  
Bursal Disease ◽  
Specific Pathogen

Infectious Bursal Disease Virus (IBDV), the etiological agent of Gumboro disease, causes mortality and immunosuppression in chickens and major losses to poultry industry worldwide. The IBDV major capsid protein VP2 is considered the best candidate for the production of novel subunit vaccines. This structural protein contains the major conformational epitopes responsible for the induction of IBDV neutralizing antibodies in chickens and has been demonstrated able to form supramolecular structures in yeast and insect cells. The aim of this study was to express an engineered version of the VP2 protein (His-pVP2) to verify its ability to self-assemble into virus-like particles in plants. The recombinant VP2 was transiently expressed by agroinfiltration in Nicotiana benthamiana and transmission electron microscopy of sucrose density gradient fractions revealed the presence of a mixed population of differently shaped particles ranging from spherical capsids, with a diameter between ~25 and ~70 nm, to tubular structures, with variable length (from 100 to 400 nm). The recombinant VP2-based particles when used for the intramuscular immunization of specific-pathogen-free chicks resulted able to induce the production of anti-IBDV specific antibodies at titers comparable to those induced by a commercial vaccine. Moreover, all the immunized birds survived to the challenge with a Moroccan very virulent IBDV strain with no major histomorphological alterations of the Bursa of Fabricius, similarly to what obtained with the commercial inactivated vaccine.

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.

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