ArticleMicrobial cell factories2017
Construct design, production, and characterization of Plasmodium falciparum 48/45 R0.6C subunit protein produced in Lactococcus lactis as candidate vaccine.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 44 citations in OpenAlex.
- A Pfs48/45-based vaccine to block Plasmodium falciparum transmission: phase 1, open-label, clinical trial.BMC medicine · 2024Trial
- Functionality of Toxoplasma gondii antibodies in a population of Beninese pregnant women exposed to malaria.Scientific reports · 2025Article
- Mucosal Administration ofJournal of microbiology and biotechnology · 2024Article
- mRNA vaccines expressing malaria transmission-blocking antigens Pfs25 and Pfs230D1 induce a functional immune response.NPJ vaccines · 2024Article
- Highly potent, naturally acquired human monoclonal antibodies against Pfs48/45 block Plasmodium falciparum transmission to mosquitoes.Immunity · 2023Article
- A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine.Immunity · 2023Article
- Quantification of Acute and Chronic Theileriosis in Sheep by Quantitative PCR (qPCR).Archives of Razi Institute · 2023Article
- Current approaches to malaria vaccines.Current opinion in microbiology · 2022Review
- Recombinant vaccines in 2022: a perspective from the cell factory.Microbial cell factories · 2022Review
- 40 Years of Pfs48/45 Research as a Transmission-Blocking Vaccine Target of Plasmodium falciparum Malaria.The American journal of tropical medicine and hygiene · 2022Article
- Method for Production of Cysteine-Rich Proteins in Lactococcus lactis Expression System.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Heterologous Expression and Evaluation of NovelFrontiers in immunology · 2022Article
- Review
- Process development and preclinical evaluation of a majorFrontiers in immunology · 2022Article
- Molecular interactions between parasite and mosquito during midgut invasion as targets to block malaria transmission.NPJ vaccines · 2021Review
- Preclinical development of a Pfs230-Pfs48/45 chimeric malaria transmission-blocking vaccine.NPJ vaccines · 2021Article
- Novel Simple Conjugation Chemistries for Decoration of GMMA with Heterologous Antigens.International journal of molecular sciences · 2021Article
- A comparative study of single Theileria lestoquardi and mixed infections with Theileria ovis.Parasites & vectors · 2021Article
- Transmission-Blocking Vaccines: Harnessing Herd Immunity for Malaria Elimination.Expert review of vaccines · 2021Review
- A cutting-edge immunoinformatics approach for design of multi-epitope oral vaccine against dreadful human malaria.International journal of biological macromolecules · 2020Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe sexual stages of Plasmodium falciparum are responsible for the spread of the parasite in malaria endemic areas. The cysteine-rich Pfs48/45 protein, exposed on the surface of sexual stages, is one of the most advanced antigens for inclusion into a vaccine that will block transmission. However, clinical Pfs48/45 sub-unit vaccine development has been hampered by the inability to produce high yields of recombinant protein as the native structure is required for the induction of functional transmission-blocking (TB) antibodies. We have investigated a downstream purification process of a sub-unit (R0.6C) fragment representing the C-terminal 6-Cys domain of Pfs48/45 (6C) genetically fused to the R0 region (R0) of asexual stage Glutamate Rich Protein expressed in Lactococcus lactis.
resultsA series of R0.6C fusion proteins containing features, which aim to increase expression levels or to facilitate protein purification, were evaluated at small scale. None of these modifications affected the overall yield of recombinant protein. Consequently, R0.6C with a C-terminal his tag was used for upstream and downstream process development. A simple work-flow was developed consisting of batch fermentation followed by two purification steps. As such, the recombinant protein was purified to homogeneity. The composition of the final product was verified by HPLC, mass spectrometry, SDS-PAGE and Western blotting with conformation dependent antibodies against Pfs48/45. The recombinant protein induced high levels of functional TB antibodies in rats.
conclusionsThe established production and purification process of the R0.6C fusion protein provide a strong basis for further clinical development of this candidate transmission blocking malaria vaccine.
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