ArticleThe Journal of biological chemistry2013
Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique interdomain organization and the potential for an antiparallel arrangement with Pf41.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- A structure-based epitope tagging approach identifies vulnerable sites on the malarial P36-P52 protein complex for antibody-mediated neutralization of Plasmodium sporozoites.PLoS pathogens · 2026Article
- Conserved genetic and antigenic profiles of Pf12 and Pf41 in asymptomatic Plasmodium falciparum carriers in Tanzania.Scientific reports · 2026Article
- Genetic diversity and natural selection of Plasmodium falciparum Pf41 vaccine candidate in clinical isolates from Senegal.Scientific reports · 2025Article
- Article
- A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine.Immunity · 2023Article
- FT-GPI, a highly sensitive and accurate predictor of GPI-anchored proteins, reveals the composition and evolution of the GPI proteome in Plasmodium species.Malaria journal · 2023Article
- 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
- Structure of the Pf12 and Pf41 heterodimeric complex ofFEMS microbes · 2022Article
- Review
- 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
- 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
- Peripheral Merozoite Surface Proteins Are Targets of Naturally Acquired Immunity against Malaria in both India and Ghana.Infection and immunity · 2020Article
- Article
- A C-terminal Pfs48/45 malaria transmission-blocking vaccine candidate produced in the baculovirus expression system.Scientific reports · 2020Article
- Malaria.tools-comparative genomic and transcriptomic database for Plasmodium species.Nucleic acids research · 2020Article
- Article
- Structural delineation of potent transmission-blocking epitope I on malaria antigen Pfs48/45.Nature communications · 2018Article
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Authors and funding
10 authors.
Funding
Abstract
Plasmodium falciparum is the most devastating agent of human malaria. A major contributor to its virulence is a complex lifecycle with multiple parasite forms, each presenting a different repertoire of surface antigens. Importantly, members of the 6-Cys s48/45 family of proteins are found on the surface of P. falciparum in every stage, and several of these antigens have been investigated as vaccine targets. Pf12 is the archetypal member of the 6-Cys protein family, containing just two s48/45 domains, whereas other members have up to 14 of these domains. Pf12 is strongly recognized by immune sera from naturally infected patients. Here we show that Pf12 is highly conserved and under purifying selection. Immunofluorescence data reveals a punctate staining pattern with an apical organization in late schizonts. Together, these data are consistent with an important functional role for Pf12 in parasite-host cell attachment or invasion. To infer the structural and functional diversity between Pf12 and the other 11 6-Cys domain proteins, we solved the 1.90 Å resolution crystal structure of the Pf12 ectodomain. Structural analysis reveals a unique organization between the membrane proximal and membrane distal domains and clear homology with the SRS-domain containing proteins of Toxoplasma gondii. Cross-linking and mass spectrometry confirm the previously identified Pf12-Pf41 heterodimeric complex, and analysis of individual cross-links supports an unexpected antiparallel organization. Collectively, the localization and structure of Pf12 and details of its interaction with Pf41 reveal important insight into the structural and functional properties of this archetypal member of the 6-Cys protein family.
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