ArticleEukaryotic cell2012
Analysis of the conformation and function of the Plasmodium falciparum merozoite proteins MTRAP and PTRAMP.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Semaphorin-7A is an erythrocyte receptor for P. falciparum merozoite-specific TRAP homolog, MTRAP.PLoS pathogens · 2012Trial
- Helminth coinfections mitigate clinical, parasitological, and immune outcomes in Mozambican children with malaria.BMC medicine · 2026Article
- Characterization of merozoite-specific thrombospondin-related anonymous protein (MTRAP) inFrontiers in cellular and infection microbiology · 2024Article
- Plasmodium vivax merozoite-specific thrombospondin-related anonymous protein (PvMTRAP) interacts with human CD36, suggesting a novel ligand-receptor interaction for reticulocyte invasion.Parasites & vectors · 2023Article
- Structural and immunological differences in Plasmodium falciparum sexual stage transmission-blocking vaccines comprised of Pfs25-EPA nanoparticles.NPJ vaccines · 2023Article
- PCRCR complex is essential for invasion of human erythrocytes by Plasmodium falciparum.Nature microbiology · 2022Article
- Thrombospondin Related Anonymous Protein Superfamily in Vector-Borne Apicomplexans: The Parasite's Toolkit for Cell Invasion.Frontiers in cellular and infection microbiology · 2022Review
- Article
- The disruption of GDP-fucose de novo biosynthesis suggests the presence of a novel fucose-containing glycoconjugate in Plasmodium asexual blood stages.Scientific reports · 2016Article
- Plasmodium Merozoite TRAP Family Protein Is Essential for Vacuole Membrane Disruption and Gamete Egress from Erythrocytes.Cell host & microbe · 2016Article
- Structural and Immunological Characterization of Recombinant 6-Cysteine Domains of the Plasmodium falciparum Sexual Stage Protein Pfs230.The Journal of biological chemistry · 2016Article
- VAR2CSA Domain-Specific Analysis of Naturally Acquired Functional Antibodies to Plasmodium falciparum Placental Malaria.The Journal of infectious diseases · 2016Article
- Red cell receptors as access points for malaria infection.Current opinion in hematology · 2016Review
- The mechanics of malaria parasite invasion of the human erythrocyte - towards a reassessment of the host cell contribution.Cellular microbiology · 2016Review
- The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by Phosphorylation.PloS one · 2016Article
- Sugar activation and glycosylation in Plasmodium.Malaria journal · 2015Review
- Plasmodium falciparum aldolase and the C-terminal cytoplasmic domain of certain apical organellar proteins promote actin polymerization.Molecular and biochemical parasitology · 2014Review
- Malaria adhesins: structure and function.Cellular microbiology · 2014Review
- Identifying novel Plasmodium falciparum erythrocyte invasion receptors using systematic extracellular protein interaction screens.Cellular microbiology · 2013Review
- Overcoming allelic specificity by immunization with five allelic forms of Plasmodium falciparum apical membrane antigen 1.Infection and immunity · 2013Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Thrombospondin repeat (TSR)-like domains are structures involved with cell adhesion. Plasmodium falciparum proteins containing TSR domains play crucial roles in parasite development. In particular, the preerythrocytic P. falciparum circumsporozoite protein is involved in hepatocyte invasion. The importance of these domains in two other malaria proteins, the merozoite-specific thrombospondin-related anonymous protein (MTRAP) and the thrombospondin-related apical membrane protein (PTRAMP), were assessed using near-full-length recombinant proteins composed of the extracellular domains produced in Escherichia coli. MTRAP is thought to be released from invasive organelles identified as micronemes during merozoite invasion to mediate motility and host cell invasion through an interaction with aldolase, an actin binding protein involved in the moving junction. PTRAMP function remains unknown. In this study, the conformation of recombinant MTRAP (rMTRAP) appeared to be a highly extended protein (2 nm by 33 nm, width by length, respectively), whereas rPTRAMP had a less extended structure. Using an erythrocyte binding assay, rMTRAP but not rPTRAMP bound human erythrocytes; rMTRAP binding was mediated through the TSR domain. MTRAP- and in general PTRAMP-specific antibodies failed to inhibit P. falciparum development in vitro. Altogether, MTRAP is a highly extended bifunctional protein that binds to an erythrocyte receptor and the merozoite motor.
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Registered trials
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