Immunogenicity analysis of the E. coli expressed structural protein VP1 of persistent infection foot-and-mouth disease virus

被引:2
作者
Tang, Huan [1 ,2 ]
Wang, Hailong [3 ]
Yang, Li [1 ,2 ]
Chen, Hong [1 ,2 ]
Kong, Lingbao [1 ,2 ]
Xin, Xiu [1 ,2 ]
机构
[1] Jiangxi Agr Univ, Inst Pathogen Microbiol, Coll Biol Sci & Engn, Nanchang 330045, Jiangxi, Peoples R China
[2] Jiangxi Agr Univ, Nanchang Key Lab Anim Virus & Genet Engn, Nanchang 330045, Jiangxi, Peoples R China
[3] Nanchang Univ, Affiliated Hosp 1, Ctr Expt Med, Nanchang 330045, Jiangxi, Peoples R China
基金
中国博士后科学基金;
关键词
Type O foot-And-mouth disease virus; Persistent infection; VP1 structural protein; Immunogenicity; Subunit vaccine; GENETIC-VARIATION; SEQUENCE; VACCINE; CATTLE; STRAIN;
D O I
10.1016/j.virol.2023.01.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The persistent infection of FMDV in cloven hoofed animals has made the epidemic prevention and control more difficult. VP1 is the main immunogenic protein and first candidate of vaccine development for FMDV prevention. However, the mutation of VP1 in host cell with persistent infection FMDV (PI-FMDV) caused the change of its immunogenicity. Hence, it is imperative to establish the expression system for VP1 of PI-FMDV (PI-VP1) and re-evaluate its immunogenicity. In this study, the PI-VP1 with His-tag was cloned into pET-28a vector. PI-VP1 protein was expressed and purified in E. coli, and further the antiserum of immunized mice was analyzed. Re -sults showed that purified PI-VP1 protein produced a good humoral and cellular immune response after immunizing mice. Furthermore, our study showed that the antiserum could not only neutralize PI-FMDV, but also prevent the adsorption of WT-FMDV. In summarize, our work provides valuable implications for the FMDV vaccines and therapeutics development.
引用
收藏
页码:111 / 118
页数:8
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