您好，欢迎访问河南省农业科学院 机构知识库！
河南省农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

PCV cap proteins fused with calreticulin expressed into polymers inEscherichia coliwith high immunogenicity in mice

文献类型： 外文期刊

作者： Liu, Chang 1 ; Liu, Yunchao 1 ; Feng, Hua 1 ; Zhao, Baolei 2 ; Chen, Yumei 3 ; Huang, Huimin 2 ; Wang, Pan 1 ; Deng, Ruig 1 ;

作者机构： 1.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Minist Agr, Key Lab Anim Immunol, Zhengzhou 450002, Henan, Peoples R China

2.Henan Agr Univ, Coll Anim Sci & Vet Med, Zhengzhou 450002, Henan, Peoples R China

3.Zhengzhou Univ, Sch Life Sci, Zhengzhou 450001, Peoples R China

关键词： Porcine circovirus type 2; CRT-cap fusion protein; Escherichia coli; Polymers; Immunogenicity

期刊名称：BMC VETERINARY RESEARCH （ 影响因子：2.741； 五年影响因子：2.955 ）

ISSN：

年卷期： 2020 年 16 卷 1 期

页码：

收录情况： SCI

摘要： Background Porcine circovirus type 2 (PCV2) is the main causative agent of porcine circovirus diseases (PCVDs) which causes huge yearly economic losses in the swine industry. Capsid protein (Cap) is the major structural protein of PCV2 that can induce a protective immune response. Therefore, developing a novel and safe subunit vaccine against PCV2 infection is needed. Results In this study, theCapgene was bound to the truncatedcalreticulin(CRT) (120-250 aa/120-308 aa) at the N/C terminal, and then the CRT-Cap fusion genes were expressed inEscherichia coli (E.coli). The size-exclusion chromatography and dynamic light scattering (DLS) data showed that the purified recombinant CRT-Cap fusion protein (rP5F) existed in the form of polymers. Immunization with rP5F stimulated high levels of PCV2 specific antibody and neutralization antibody in mice, which were almost identical to those induced by the commercial subunit and inactivated vaccines. The lymphocyte proliferation and cytokine secretion were also detected in rP5F immunized mice. According to the results of PCV2-challenge experiment, the virus loads significantly decreased in mice immunized with rP5F. The data obtained in the current study revealed that rP5F had the potential to be a subunit vaccine candidate against PCV2 in the future. Conclusions We have successfully expressed Cap-CRT fusion proteins inE.coliand optimized rP5F could form into immunogenic polymers. Mice immunized with rP5F efficiently induced humoral and part of cellular immune responses and decreased the virus content against PCV2-challenge, which suggested that rF5P could be a potential subunit vaccine candidate.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：河南省农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台