Small interfering RNAs inhibit infectious bursal disease virus replication in Vero cells

2011 ◽  
Vol 55 (1) ◽  
pp. 75-79 ◽  
Author(s):  
B. SAJJANAR ◽  
A. MISHRA ◽  
A. SONAWANE ◽  
C. PATEL ◽  
A. SAXENA ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Infectious Bursal Disease Virus ◽  
Vero Cells ◽  
Infectious Bursal Disease ◽  
Small Interfering Rnas ◽  
Bursal Disease

scholarly journals Chicken Heat Shock Protein 70 Is an Essential Host Protein for Infectious Bursal Disease Virus Infection In Vitro

Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 664
Author(s):  
Yufang Meng ◽  
Xiaoxue Yu ◽  
Chunxue You ◽  
Wenjuan Zhang ◽  
Yingfeng Sun ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Disease Virus ◽  
Heat Shock Protein 70 ◽  
Infectious Bursal Disease Virus ◽  
Host Protein ◽  
Infectious Bursal Disease ◽  
Economic Losses ◽  
Small Interfering Rnas ◽  
Bursal Disease

Infectious bursal disease virus (IBDV) infection causes pathogenicity and mortality in chickens, leading to huge economic losses in the poultry industry worldwide. Studies of host-virus interaction can help us to better understand the viral pathogenicity. As a highly conservative host factor, heat shock protein 70 (Hsp70) is observed to be involved in numerous viral infections. However, there is little information about the role of chicken Hsp70 (cHsp70) in IBDV infection. In the present study, the increased expression of cHsp70 was observed during IBDV-infected DF-1 cells. Further studies revealed that Hsp70 had similar locations with the viral double-stranded RNA (dsRNA), and the result of pull-down assay showed the direct interaction between cHsp70 with dsRNA, viral proteins (vp)2 and 3, indicating that maybe cHsp70 participates in the formation of the replication and transcription complex. Furthermore, overexpression of cHsp70 promoted IBDV production and knockdown of cHsp70 using small interfering RNAs (siRNA) and reducedviral production, implying the necessity of cHsp70 in IBDV infection. These results reveal that cHsp70 is essential for IBDV infection in DF-1 cells, suggesting that targeting cHsp70 may be applied as an antiviral strategy.

scholarly journals Immunogenicity and Efficacy Evaluation of Vero Cell-Adapted Infectious Bursal Disease Virus LC-75 Vaccine Strain in Ethiopia 

2021 ◽  
Author(s):  
Wakjira Kebebe ◽  
Molalegne Bitew ◽  
Fufa Dawo ◽  
Bedaso Mammo ◽  
Hawa Mohammed ◽  
...  
Keyword(s):  
Vero Cell ◽  
Disease Virus ◽  
Vaccine Strain ◽  
Infectious Bursal Disease Virus ◽  
Chicken Embryo Fibroblast ◽  
Vero Cells ◽  
Infectious Bursal Disease ◽  
Efficacy Evaluation ◽  
Viral Pathogen ◽  
Bursal Disease

Abstract Background: Infectious bursal disease virus (IBDV) is an avian viral pathogen that causes infectious bursal disease (IBD) of chickens. The disease is endemic in Ethiopia since 2002 and vaccination is the major means of disease prevention and control. IBD vaccine is produced in Ethiopia using primary chicken embryo fibroblast (CEF) cell; which is time-consuming, laborious, and uneconomical. The present study was carried out to develop cell-based IBDV LC-75 vaccine using Vero cells, and to evaluate the immunogenicity and protection level.Results: Identity of the vaccine seed was confirmed using gene-specific primers using reverse transcription polymerase chain reaction. Confluent monolayer of Vero cells was infected with vaccine virus and serial passage continued till passage ten. Characteristic virus induced cytopathic effect was observed starting from passage 2 on the third day post-infection. The infectious titer of adapted virus showed a linear increment along the passage level. Virus induced specific antibody was determined using indirect ELISA after vaccination of 14 days old chicks through ocular route. Accordingly, the antibody titer measured from Vero cells vaccinated chicks revealed similar level with the currently available CEF cell-based vaccine. Chicks vaccinated with Vero cell adapted virus showed complete protection against very virulent IBDV, while unvaccinated group had 60% morbidity and 25% mortality.Conclusions: The IBDV vaccine strain well adapted on Vero cells and found to be immunogenic induces antibodies development and successfully protects chicks against challenging with the circulating field IBDV isolate. Hence, it is recommended to produce IBD vaccine using Vero cell culture with enough quantity to conquer the limitations using CEF cells and thus to vaccinate chicks to protect against IBDV infection.

Reduction of infectious bursal disease virus replication by shRNAs targeting the VP1 and VP2 genes driven by chicken U6 promoter

2013 ◽  
Vol 162 (1) ◽  
pp. 44-52 ◽  
Author(s):  
Wei Ouyang ◽  
Jin-rong Ma ◽  
Yong-qiang Wang ◽  
Li-ting Qin ◽  
Jie-yuan Jiang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Infectious Bursal Disease Virus ◽  
Infectious Bursal Disease ◽  
U6 Promoter ◽  
Bursal Disease

Demonstration of receptor binding properties of VP2 of very virulent strain infectious bursal disease virus on Vero cells

2007 ◽  
Vol 123 (1) ◽  
pp. 50-56 ◽  
Author(s):  
Chi Wai Yip ◽  
Yin Shan Yeung ◽  
Ching Man Ma ◽  
Pui Yi Lam ◽  
Chung Chau Hon ◽  
...  
Keyword(s):  
Disease Virus ◽  
Receptor Binding ◽  
Infectious Bursal Disease Virus ◽  
Virulent Strain ◽  
Vero Cells ◽  
Infectious Bursal Disease ◽  
Binding Properties ◽  
Bursal Disease

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.

scholarly journals Cyclophilin A Interacts with Viral VP4 and Inhibits the Replication of Infectious Bursal Disease Virus

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Nian Wang ◽  
Lizhou Zhang ◽  
Yuming Chen ◽  
Zhen Lu ◽  
Li Gao ◽  
...  
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Nonstructural Protein ◽  
Chicken Embryo Fibroblast ◽  
Cyclophilin A ◽  
Host Cells ◽  
Infectious Bursal Disease ◽  
Cell Protein ◽  
Small Interfering Rnas ◽  
Bursal Disease

Nonstructural protein VP4, a serine protease of infectious bursal disease virus (IBDV) that catalyzes the hydrolysis of polyprotein pVP2-VP4-VP3 to form the viral proteins VP2, VP4, and VP3, is essential to the replication of IBDV. However, the interacting partners of VP4 in host cells and the effects of the interaction on the IBDV lifecycle remain incompletely elucidated. In this study, using the yeast two-hybrid system, the putative VP4-interacting partner cyclophilin A (CypA) was obtained from a chicken embryo fibroblast (CEF) expression library. CypA was further confirmed to interact with VP4 of IBDV using co-immunoprecipitation (CO-IP), GST pull-down, and confocal microscopy assays. Moreover, we found that the overexpression of CypA suppressed IBDV replication, whereas the knock-down of CypA by small interfering RNAs promoted the replication of IBDV. Taken together, our findings indicate that the host cell protein CypA interacts with viral VP4 and inhibits the replication of IBDV.

Sign in / Sign up

Export Citation Format

Share Document