ArticleScientific reports2022
Structural analysis of Plasmodium falciparum ookinete surface antigen Pfs28 relevant for malaria vaccine design.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Nanocarrier-based immunotherapy for viral diseases.International journal of pharmaceutics: X · 2025Review
- Computational Development of Transmission-Blocking Vaccine Candidates Based on Fused Antigens of Pre- and Post-fertilization Gametocytes AgainstBioinformatics and biology insights · 2025Article
- Multi-locus investigation of Anopheles-mediated selective pressure on Plasmodium falciparum in Africa.Parasites & vectors · 2024Article
- Diversity and selection analyses identify transmission-blocking antigens as the optimal vaccine candidates in Plasmodium falciparum.EBioMedicine · 2024Article
- To each its own: Mechanisms of cross-talk between GPI biosynthesis and cAMP-PKA signaling in Candida albicans versus Saccharomyces cerevisiae.The Journal of biological chemistry · 2024Review
- Diversity and selection analyses identify transmission-blocking antigens as the optimal vaccine candidates inmedRxiv : the preprint server for health sciences · 2024Article
- A potent and durable malaria transmission-blocking vaccine designed from a single-component 60-copy Pfs230D1 nanoparticle.NPJ vaccines · 2023Article
- A human antibody epitope map of the malaria vaccine antigen Pfs25.NPJ vaccines · 2023Article
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Authors and funding
3 authors.
Funding
Abstract
Pfs28 is a Plasmodium falciparum malaria transmission-blocking vaccine candidate that is anchored to the parasite surface through a C-terminal glycosylphosphatidylinositol (GPI) moiety, and plays a role in parasite survival in the mosquito midgut. Pfs28 contains epidermal growth factor (EGF)-like domains and is part of a family of sexual stage malaria proteins that includes the related vaccine antigen Pfs25. The lack of structural definition of Pfs28 and the immune response to this candidate has limited further malaria vaccine development for this antigen. Here, we present the crystal structure of Pfs28, examine its conservation with P. vivax Pvs28, and evaluate the cross-reactivity of Pfs28 to antibodies that recognize Pfs25. Pfs28 is comprised of four EGF-like domains stabilized by ten disulfide bridges with an overall architecture that highly resembles Pfs25. Despite the high sequence and structural similarity between these antigens, no cross reactivity of Pfs28 to anti-Pfs25 monoclonal antibodies could be demonstrated.
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