Production of Plasmodium vivax Enolase in Escherichia coli and its Protective Properties
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- 英文论文题名：Production of Plasmodium vivax Enolase in Escherichia coli and its Protective Properties
- 论文作者：Chao Zhang ; Yaping Gu ; Jianxia Tang ; Feng Lu ; Yuanyuan Cao ; Huayun Zhou ; Guoding Zhu ; Jun Cao ; Qi Gao
- 英文论文作者：Chao Zhang ; Yaping Gu ; Jianxia Tang ; Feng Lu ; Yuanyuan Cao ; Huayun Zhou ; Guoding Zhu ; Jun Cao ; Qi Gao ; Key Laboratory on Technology for Disease Prevention and Control(Ministry of Health) ; Jiangsu Provincial Key Laboratory on Parasite and Vector Control Technology ; Jiangsu Institute of Parasitic Diseases ; Public Health Research Center ; Jiangnan University
- 年：2016
- 作者机构：Key Laboratory on Technology for Disease Prevention and Control(Ministry of Health), Jiangsu Provincial Key Laboratory on Parasite and Vector Control Technology, Jiangsu Institute of Parasitic Diseases;Public Health Research Center, Jiangnan University;
- 英文论文关键词：Malaria ; Plasmodium vivax ; Enolase ; Prokaryotic expression ; Vaccine candidate
- 会议召开时间：2016-08-08
- 会议录名称：中国动物学会寄生虫学专业委员会第十届全国寄生虫学青年工作者学术研讨会论文摘要集
- 英文会议录名称：The Abstracts of the Tenth Symposium for Yong Scientists of China Society of Parasitology
- 语种：英文
- 分类号：R531
- 学会代码：JISC
- 会议名称：中国动物学会寄生虫学专业委员会第十届全国寄生虫学青年工作者学术研讨会
- 会议地点：中国四川成都
- 主办单位：中国动物学会寄生虫学专业青年委员会
- 学会名称：中国动物学会寄生虫学专业委员会
- 页数：1
- 文件大小：157k
- 原文格式：D
- 会议级别：全国
摘要
Objective: Plasmodium vivax predominates in South-East Asia and the American continent, causes significant morbidity and inflicts a huge socioeconomic burden. Sequencing completion of the Plasmodium vivax genome and transcriptome provides the chance to identify antigens. Enolase is the eighth enzyme in the glycolytic pathway, which, apart from its glycolytic function, also possess antigenic properties and is present on the cell wall of many invasive organisms, such as Candida albicans. In order to assess whether enolase of Plasmodium vivax is also antigenic, in this study, we first reported the expression and purification of recombinant Plasmodium vivax enolase(r-Pven) in Escherichia coli, using prokaryotic expression vector. Methods and results: The r-Pven was expressed in soluble form in E. coli, and the expression was verified by SDS-PAGE and western blotting analysis. The r-Pven was purified to 90% purity by nickel–nitrilotriacetic acid(Ni~(2+)–NTA) resin chromatography. For reactivity with r-Pven, compared with the average values of the reactivity of control serum samples, the average values of the reactivity of 99 individual serums from vivax malaria patients appeared higher, and there was significant difference between them(p=0.0117<0.05). Mice anti-r-Pven antibodies inhibited the growth of in vitro cultures of P. falciparum. Mice immunized with r-Pven showed protection against a challenge with the mouse malarial parasite Plasmodium berghei. The antibodies raised against r-Pven were specific for Plasmodium and did not react to the host tissues. Conclusion: These observations established Plasmodium vivax enolase to be a potential protective antigen.
Objective: Plasmodium vivax predominates in South-East Asia and the American continent, causes significant morbidity and inflicts a huge socioeconomic burden. Sequencing completion of the Plasmodium vivax genome and transcriptome provides the chance to identify antigens. Enolase is the eighth enzyme in the glycolytic pathway, which, apart from its glycolytic function, also possess antigenic properties and is present on the cell wall of many invasive organisms, such as Candida albicans. In order to assess whether enolase of Plasmodium vivax is also antigenic, in this study, we first reported the expression and purification of recombinant Plasmodium vivax enolase(r-Pven) in Escherichia coli, using prokaryotic expression vector. Methods and results: The r-Pven was expressed in soluble form in E. coli, and the expression was verified by SDS-PAGE and western blotting analysis. The r-Pven was purified to 90% purity by nickel–nitrilotriacetic acid(Ni~(2+)–NTA) resin chromatography. For reactivity with r-Pven, compared with the average values of the reactivity of control serum samples, the average values of the reactivity of 99 individual serums from vivax malaria patients appeared higher, and there was significant difference between them(p=0.0117<0.05). Mice anti-r-Pven antibodies inhibited the growth of in vitro cultures of P. falciparum. Mice immunized with r-Pven showed protection against a challenge with the mouse malarial parasite Plasmodium berghei. The antibodies raised against r-Pven were specific for Plasmodium and did not react to the host tissues. Conclusion: These observations established Plasmodium vivax enolase to be a potential protective antigen.
Objective: Plasmodium vivax predominates in South-East Asia and the American continent, causes significant morbidity and inflicts a huge socioeconomic burden. Sequencing completion of the Plasmodium vivax genome and transcriptome provides the chance to identify antigens. Enolase is the eighth enzyme in the glycolytic pathway, which, apart from its glycolytic function, also possess antigenic properties and is present on the cell wall of many invasive organisms, such as Candida albicans. In order to assess whether enolase of Plasmodium vivax is also antigenic, in this study, we first reported the expression and purification of recombinant Plasmodium vivax enolase(r-Pven) in Escherichia coli, using prokaryotic expression vector. Methods and results: The r-Pven was expressed in soluble form in E. coli, and the expression was verified by SDS-PAGE and western blotting analysis. The r-Pven was purified to 90% purity by nickel–nitrilotriacetic acid(Ni~(2+)–NTA) resin chromatography. For reactivity with r-Pven, compared with the average values of the reactivity of control serum samples, the average values of the reactivity of 99 individual serums from vivax malaria patients appeared higher, and there was significant difference between them(p=0.0117<0.05). Mice anti-r-Pven antibodies inhibited the growth of in vitro cultures of P. falciparum. Mice immunized with r-Pven showed protection against a challenge with the mouse malarial parasite Plasmodium berghei. The antibodies raised against r-Pven were specific for Plasmodium and did not react to the host tissues. Conclusion: These observations established Plasmodium vivax enolase to be a potential protective antigen.
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