ArticleThe Journal of biological chemistry2009
Structure of the Plasmodium falciparum circumsporozoite protein, a leading malaria vaccine candidate.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed, 160 citations in OpenAlex.
- Longitudinal analysis of naturally acquired PfEMP1 CIDR domain variant antibodies identifies associations with malaria protection.JCI insight · 2020Trial
- Immunization of Malaria-Preexposed Volunteers With PfSPZ Vaccine Elicits Long-Lived IgM Invasion-Inhibitory and Complement-Fixing Antibodies.The Journal of infectious diseases · 2018Trial
- Monoclonal antibody CIS43LS sets the bar for long-acting malaria protection.The Journal of clinical investigation · 2026Article
- Machine learning enables de novo multiepitope design ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Plasmodium CSP repeats have elastic properties with a critical role in sporozoite motility.The EMBO journal · 2025Article
- Genetic diversity and natural selection of circumsporozoite surface protein in Vietnam Plasmodium falciparum isolates.Malaria journal · 2025Article
- Comparison of major, minor and junctional circumsporozoite protein epitopes for malaria vaccine design.NPJ vaccines · 2025Article
- Virus-like particle vaccines targeting a key epitope in circumsporozoite protein provide sterilizing immunity against malaria.NPJ vaccines · 2025Article
- Article
- Elicitation of liver-stage immunity by nanoparticle immunogens displaying P. falciparum CSP-derived antigens.NPJ vaccines · 2025Article
- Distinct evolutionary regimes across domains of the Plasmodium falciparum CSP gene.Scientific reports · 2025Article
- The Plasmodium circumsporozoite protein.Trends in parasitology · 2024Review
- Monoclonal antibodies to the circumsporozoite proteins as an emerging tool for malaria prevention.Nature immunology · 2024Review
- Genetic polymorphism and evidence of signatures of selection in the Plasmodium falciparum circumsporozoite protein gene in Tanzanian regions with different malaria endemicity.Malaria journal · 2024Article
- Design and Evaluation of ChimericVaccines · 2024Article
- Genetic polymorphism and evidence of signatures of selection in themedRxiv : the preprint server for health sciences · 2024Article
- Production and Purification of Plasmodium Circumsporozoite Protein in Lactococcus lactis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain.Protein science : a publication of the Protein Society · 2024Article
- Malaria & mRNA Vaccines: A Possible Salvation from One of the Most Relevant Infectious Diseases of the Global South.Acta parasitologica · 2023Article
- Affinity-matured homotypic interactions induce spectrum of PfCSP structures that influence protection from malaria infection.Nature communications · 2023Article
50 more citing papers are in PubMed but not listed here.
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Authors and funding
20 authors at 3 institutions in 1 country.
Funding
Abstract
The Plasmodium falciparum circumsporozoite protein (CSP) is critical for sporozoite function and invasion of hepatocytes. Given its critical nature, a phase III human CSP malaria vaccine trial is ongoing. The CSP is composed of three regions as follows: an N terminus that binds heparin sulfate proteoglycans, a four amino acid repeat region (NANP), and a C terminus that contains a thrombospondin-like type I repeat (TSR) domain. Despite the importance of CSP, little is known about its structure. Therefore, recombinant forms of CSP were produced by expression in both Escherichia coli (Ec) and then refolded (EcCSP) or in the methylotrophic yeast Pichia pastoris (PpCSP) for structural analyses. To analyze the TSR domain of recombinant CSP, conformation-dependent monoclonal antibodies that recognized unfixed P. falciparum sporozoites and inhibited sporozoite invasion of HepG2 cells in vitro were identified. These monoclonal antibodies recognized all recombinant CSPs, indicating the recombinant CSPs contain a properly folded TSR domain structure. Characterization of both EcCSP and PpCSP by dynamic light scattering and velocity sedimentation demonstrated that both forms of CSP appeared as highly extended proteins (R(h) 4.2 and 4.58 nm, respectively). Furthermore, high resolution atomic force microscopy revealed flexible, rod-like structures with a ribbon-like appearance. Using this information, we modeled the NANP repeat and TSR domain of CSP. Consistent with the biochemical and biophysical results, the repeat region formed a rod-like structure about 21-25 nm in length and 1.5 nm in width. Thus native CSP appears as a glycosylphosphatidylinositol-anchored, flexible rod-like protein on the sporozoite surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.