ArticleHuman vaccines & immunotherapeutics2016
Production of Plasmodium vivax enolase in Escherichia coli and its protective properties.
Article in Human vaccines & immunotherapeutics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Enolase AmEno15, a Promising Candidate for Understanding the Infectious Process ofInternational journal of molecular sciences · 2025Article
- Plasmodium vivax tryptophan-rich antigen reduces type I collagen secretion via the NF-κBp65 pathway in splenic fibroblasts.Parasites & vectors · 2024Article
- An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein.Frontiers in veterinary science · 2023Article
- Complete Molecular and Immunoprotective Characterization ofFrontiers in microbiology · 2017Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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. 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
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