Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin (R)

CORC > 厦门大学 > 生命科学－已发表论文

	Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin (R)
	Zhang, Xiao ; Wei, Minxi ; Pan, Huirong ; Lin, Zhijie ; Wang, Kaihang ; Weng, Zusen ; Zhu, Yibin ; Xin, Lu ; Zhang, Jun ; Li, Shaowei ; Xia, Ningshao ; Zhao, Qinjian ; Zhang J(张军) ; Li SW(李少伟) ; Xia NS(夏宁邵) ; Zhao QJ(赵勤俭)
刊名	http://dx.doi.org/10.1016/j.vaccine.2014.05.064
	2014-07-07
关键词	E VACCINE MONOCLONAL-ANTIBODIES REDOX-TREATMENT CAPSID PROTEIN IMMUNOGENICITY NEUTRALIZATION ANTIGENICITY MATURATION PRIMATES EFFICACY
英文摘要	China Ministry of Science and Technology via the Major Project [2012AA02A408]; National Science Fund [81373061]; Fujian Provincial Science Fund for Distinguished Young Scholars [2011J06015]; Institute Reconstruction Fund [2011FU125Z04]; The hepatitis E virus (HEV) vaccine, Hecolin (R), was licensed in China for the prevention of HEV infection and HEV-related diseases with demonstrated safety and efficacy [1,2]. The vaccine is composed of a truncated REV capsid protein, p239, as the sole antigen encoded by open reading frame 2 and produced using Escherichia coli platform. The production of this virus-like particle (VLP) form of the antigen was successfully scaled up 50-fold from a bench scale to a manufacturing scale. Product consistency was demonstrated using a combination of biophysical, biochemical and immunochemical methods, which revealed comparable antigen characteristics among different batches. Particle size of the nanometer scale particulate antigen and presence of key epitopes on the particle surface are two prerequisites for an efficacious VLP-based vaccine. The particle size was monitored by several different methods, which showed diameters between 20 and 30 nm for the p239 particles. The thermal stability and aggregation propensity of the antigen were assessed using differential scanning calorimetry and cloud point assay under heat stress conditions. Key epitopes on the particulate antigen were analyzed using a panel of murine anti-REV monoclonal antibodies (mAbs). The immuno reactivity to the mAbs among the different antigen lots was highly consistent when analyzed quantitatively using a surface plasmon resonance technique. Using a sandwich ELISA to probe the integrity of two different epitopes in the antigen, the specific antigenicity of multiple batches was assessed to demonstrate consistency in these critical product attributes. Overall, our findings showed that the antigen production process is robust and scalable during the manufacturing of Hecolin (R). (C) 2014 Elsevier Ltd. All rights reserved.
语种	英语
出版者	ELSEVIER SCI LTD
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/90752]
专题	生命科学－已发表论文
推荐引用方式 GB/T 7714	Zhang, Xiao,Wei, Minxi,Pan, Huirong,et al. Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin (R)[J]. http://dx.doi.org/10.1016/j.vaccine.2014.05.064,2014.
APA	Zhang, Xiao.,Wei, Minxi.,Pan, Huirong.,Lin, Zhijie.,Wang, Kaihang.,...&赵勤俭.(2014).Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin (R).http://dx.doi.org/10.1016/j.vaccine.2014.05.064.
MLA	Zhang, Xiao,et al."Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin (R)".http://dx.doi.org/10.1016/j.vaccine.2014.05.064 (2014).