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Title: Large-scale production of foot-and-mouth disease virus (serotype Asia1) VLP vaccine in Escherichia coli and protection potency evaluation in cattle
Authors: Xiao, Y
Chen, H.-Y 
Wang, Y
Yin, B 
Lv, C
Mo, X 
Yan, H
Xuan, Y
Huang, Y
Pang, W
Li, X
Yuan, Y.A 
Tian, K.
Keywords: Antibodies
Escherichia coli
E. coli
Fifty percent protection dose (PD50)
Foot and mouth disease
Virus-like particles
capsid protein
foot and mouth disease vaccine
immunological adjuvant
neutralizing antibody
protein VP0
protein VP1
protein VP3
unclassified drug
virus like particle vaccine
recombinant protein
virus like particle vaccine
animal experiment
antibody response
antibody specificity
controlled study
drug potency
enzyme linked immunosorbent assay
Escherichia coli
foot and mouth disease
Foot and mouth disease virus
gene expression system
protein assembly
protein purification
single drug dose
batch cell culture
Cattle Diseases
Foot-and-Mouth Disease
protein engineering
Batch Cell Culture Techniques
Cattle Diseases
Escherichia coli
Foot-and-Mouth Disease
Protein Engineering
Recombinant Proteins
Vaccines, Virus-Like Particle
Issue Date: 2016
Publisher: BioMed Central Ltd.
Citation: Xiao, Y, Chen, H.-Y, Wang, Y, Yin, B, Lv, C, Mo, X, Yan, H, Xuan, Y, Huang, Y, Pang, W, Li, X, Yuan, Y.A, Tian, K. (2016). Large-scale production of foot-and-mouth disease virus (serotype Asia1) VLP vaccine in Escherichia coli and protection potency evaluation in cattle. BMC Biotechnology 16 (1) : 56. ScholarBank@NUS Repository.
Abstract: Background: Foot-and-mouth disease (FMD) is an acute, highly contagious disease that infects cloven-hoofed animals. Vaccination is an effective means of preventing and controlling FMD. Compared to conventional inactivated FMDV vaccines, the format of FMDV virus-like particles (VLPs) as a non-replicating particulate vaccine candidate is a promising alternative. Results: In this study, we have developed a co-expression system in E. coli, which drove the expression of FMDV capsid proteins (VP0, VP1, and VP3) in tandem by a single plasmid. The co-expressed FMDV capsid proteins (VP0, VP1, and VP3) were produced in large scale by fermentation at 10 L scale and the chromatographic purified capsid proteins were auto-assembled as VLPs in vitro. Cattle vaccinated with a single dose of the subunit vaccine, comprising in vitro assembled FMDV VLP and adjuvant, developed FMDV-specific antibody response (ELISA antibodies and neutralizing antibodies) with the persistent period of 6 months. Moreover, cattle vaccinated with the subunit vaccine showed the high protection potency with the 50 % bovine protective dose (PD50) reaching 11.75 PD50 per dose. Conclusions: Our data strongly suggest that in vitro assembled recombinant FMDV VLPs produced from E. coli could function as a potent FMDV vaccine candidate against FMDV Asia1 infection. Furthermore, the robust protein expression and purification approaches described here could lead to the development of industrial level large-scale production of E. coli-based VLPs against FMDV infections with different serotypes. © 2016 The Author(s).
Source Title: BMC Biotechnology
ISSN: 14726750
DOI: 10.1186/s12896-016-0285-6
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