ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the Plasmodium 6-cysteine s48/45 domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 73 citations in OpenAlex.
- Pfs48/45 nanobodies block Plasmodium falciparum transmission.PLoS pathogens · 2026Article
- A Self-Assembling Pfs230D1-Ferritin Nanoparticle Vaccine Has Potent and Durable Malaria Transmission-Reducing Activity.Vaccines · 2024Article
- Coevolutionary Analysis of the Pfs47-P47Rec Complex: A Bioinformatics Approach.Bioinformatics and biology insights · 2024Article
- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- Nanobodies against Pfs230 block Plasmodium falciparum transmission.The Biochemical journal · 2022Article
- PCRCR complex is essential for invasion of human erythrocytes by Plasmodium falciparum.Nature microbiology · 2022Article
- Pfs47 as a Malaria Transmission-Blocking Vaccine Target.The American journal of tropical medicine and hygiene · 2022Article
- On Malaria Transmission and Transmission Blocking Immunity.The American journal of tropical medicine and hygiene · 2022Article
- 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
- Structure of the Pf12 and Pf41 heterodimeric complex ofFEMS microbes · 2022Article
- Review
- Novel insights from the Plasmodium falciparum sporozoite-specific proteome by probabilistic integration of 26 studies.PLoS computational biology · 2021Article
- Nanobody generation and structural characterization of Plasmodium falciparum 6-cysteine protein Pf12p.The Biochemical journal · 2021Article
- Structural vaccinology of malaria transmission-blocking vaccines.Expert review of vaccines · 2021Review
- Profiling the Quality and Quantity of Naturally Induced Antibody Responses Against Pfs230 and Pfs48/45 Among Non-Febrile Children Living in Southern Ghana: A Longitudinal Study.Frontiers in cellular and infection microbiology · 2021Article
- A Protective and Pathogenic Role for Complement During AcuteFrontiers in cellular and infection microbiology · 2021Review
- Structure and function of a malaria transmission blocking vaccine targeting Pfs230 and Pfs230-Pfs48/45 proteins.Communications biology · 2020Article
- Getting in: The structural biology of malaria invasion.PLoS pathogens · 2019Review
- The first identification of complete Eph-ephrin signalling in ctenophores and sponges reveals a role for neofunctionalization in the emergence of signalling domains.BMC evolutionary biology · 2019Article
- Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The s48/45 domain was first noted in Plasmodium proteins more than 15 y ago. Previously believed to be unique to Plasmodium, the s48/45 domain is present in other aconoidasidans. In Plasmodium, members of the s48/45 family of proteins are localized on the surface of the parasite in different stages, mostly by glycosylphosphatydylinositol-anchoring. Members such as P52 and P36 seem to play a role in invasion of hepatocytes, and Pfs230 and Pfs48/45 are involved in fertilization in the sexual stages and have been consistently studied as targets of transmission-blocking vaccines for years. In this report, we present the molecular structure for the s48/45 domain corresponding to the C-terminal domain of the blood-stage protein Pf12 from Plasmodium falciparum, obtained by NMR. Our results indicate that this domain is a β-sandwich formed by two sheets with a mixture of parallel and antiparallel strands. Of the six conserved cysteines, two pairs link the β-sheets by two disulfide bonds, and the third pair forms a bond outside the core. The structure of the s48/45 domain conforms well to the previously defined surface antigen 1 (SAG1)-related-sequence (SRS) fold observed in the SAG family of surface antigens found in Toxoplasma gondii. Despite extreme sequence divergence, remarkable spatial conservation of one of the disulfide bonds is observed, supporting the hypothesis that the domains have evolved from a common ancestor. Furthermore, a homologous domain is present in ephrins, raising the possibility that the precursor of the s48/45 and SRS domains emerged from an ancient transfer to Apicomplexa from metazoan hosts.
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