scholarly journals Efficient self-assembly and protective efficacy of infectious bursal disease virus-like particles by a recombinant baculovirus co-expressing precursor polyprotein and VP4

2015 ◽  
Vol 12 (1) ◽  
Author(s):  
Hyun-Jeong Lee ◽  
Ji-Ye Kim ◽  
Soo-jeong Kye ◽  
Hee-Jung Seul ◽  
Suk-Chan Jung ◽  
...  
Vaccines ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 142
Author(s):  
Yulong Wang ◽  
Nan Jiang ◽  
Linjin Fan ◽  
Li Gao ◽  
Kai Li ◽  
...  

Infectious bursal disease (IBD), an immunosuppressive disease of young chickens, is caused by infectious bursal disease virus (IBDV). Novel variant IBDV (nVarIBDV), a virus that can evade immune protection against very virulent IBDV (vvIBDV), is becoming a threat to the poultry industry. Therefore, nVarIBDV-specific vaccine is much needed for nVarIBDV control. In this study, the VP2 protein of SHG19 (a representative strain of nVarIBDV) was successfully expressed using an Escherichia coli expression system and further purified via ammonium sulfate precipitation and size-exclusion chromatography. The purified protein SHG19-VP2-466 could self-assemble into 25-nm virus-like particle (VLP). Subsequently, the immunogenicity and protective effect of the SHG19-VLP vaccine were evaluated using animal experiments, which indicated that the SHG19-VLP vaccine elicited neutralization antibodies and provided 100% protection against the nVarIBDV. Furthermore, the protective efficacy of the SHG19-VLP vaccine against the vvIBDV was evaluated. Although the SHG19-VLP vaccine induced a comparatively lower vvIBDV-specific neutralization antibody titer, it provided good protection against the lethal vvIBDV. In summary, the SHG19-VLP candidate vaccine could provide complete immune protection against the homologous nVarIBDV as well as the heterologous vvIBDV. This study is of significance to the comprehensive prevention and control of the recent atypical IBD epidemic.


1994 ◽  
Vol 38 (4) ◽  
pp. 701 ◽  
Author(s):  
D. B. Snyder ◽  
V. N. Vakharia ◽  
S. A. Mengel-Whereat ◽  
G. H. Edwards ◽  
P. K. Savage ◽  
...  

1998 ◽  
Vol 79 (5) ◽  
pp. 1047-1054 ◽  
Author(s):  
A Fern√°ndez-Arias ◽  
J P Albar ◽  
S Mart√≠nez ◽  
J F Rodr√≠guez ◽  
C Risco

1999 ◽  
Vol 73 (8) ◽  
pp. 6973-6983 ◽  
Author(s):  
Eleuterio Lombardo ◽  
Antonio Maraver ◽  
José R. Castón ◽  
José Rivera ◽  
Armando Fernández-Arias ◽  
...  

ABSTRACT A cDNA corresponding to the coding region of VP1, the putative RNA-dependent RNA polymerase, of infectious bursal disease virus (IBDV) was cloned and inserted into the genome of a vaccinia virus inducible expression vector. The molecular mass and antigenic reactivity of VP1 expressed in mammalian cells are identical to those of its counterpart expressed in IBDV-infected cells. The results presented here demonstrate that VP1 is efficiently incorporated into IBDV virus-like particles (VLPs) produced in mammalian cells coexpressing the IBDV polyprotein and VP1. Incorporation of VP1 into VLPs requires neither the presence of IBDV RNAs nor that of the nonstructural polypeptide VP5. Immunofluorescence, confocal laser scanning microscopy, and immunoprecipitation analyses conclusively showed that VP1 forms complexes with the structural polypeptide VP3. Formation of VP1-VP3 complexes is likely to be a key step for the morphogenesis of IBDV particles.


Sign in / Sign up

Export Citation Format

Share Document