Trial reportPLoS pathogens2012
Semaphorin-7A is an erythrocyte receptor for P. falciparum merozoite-specific TRAP homolog, MTRAP.
Trial report in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 89 citations in OpenAlex.
- A Library of Plasmodium vivax Recombinant Merozoite Proteins Reveals New Vaccine Candidates and Protein-Protein Interactions.PLoS neglected tropical diseases · 2015Trial
- Comparative genomics, integrated with single-cell sequencing and genetic analyses, reveal roles of transcription factor AP2-M2 in asexual replication of Babesia parasite.PLoS pathogens · 2025Article
- Development of an improved blood-stage malaria vaccine targeting the essential RH5-CyRPA-RIPR invasion complex.Nature communications · 2024Article
- A panel of recombinantmBio · 2024Article
- 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
- Vivaxin genes encode highly immunogenic, non-variant antigens on the Trypanosoma vivax cell-surface.PLoS neglected tropical diseases · 2022Article
- Thrombospondin Related Anonymous Protein Superfamily in Vector-Borne Apicomplexans: The Parasite's Toolkit for Cell Invasion.Frontiers in cellular and infection microbiology · 2022Review
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- Structural organization of erythrocyte membrane microdomains and their relation with malaria susceptibility.Communications biology · 2021Article
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- Proteome of Stored RBC Membrane and Vesicles from Heterozygous Beta Thalassemia Donors.International journal of molecular sciences · 2021Article
- Control of oviductal fluid flow by the G-protein coupled receptor Adgrd1 is essential for murine embryo transit.Nature communications · 2021Article
- Article
- Characterization of the erythrocyte GTPase Rac1 in relation to Plasmodium falciparum invasion.Scientific reports · 2020Article
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- Rapid and sensitive large-scale screening of low affinity extracellular receptor protein interactions by using reaction induced inhibition of Gaussia luciferase.Scientific reports · 2020Article
- Antibodies against a short region of PfRipr inhibit Plasmodium falciparum merozoite invasion and PfRipr interaction with Rh5 and SEMA7A.Scientific reports · 2020Article
- Resurrection of the ancestral RH5 invasion ligand provides a molecular explanation for the origin of P. falciparum malaria in humans.PLoS biology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The motility and invasion of Plasmodium parasites is believed to require a cytoplasmic actin-myosin motor associated with a cell surface ligand belonging to the TRAP (thrombospondin-related anonymous protein) family. Current models of invasion usually invoke the existence of specific receptors for the TRAP-family ligands on the surface of the host cell; however, the identities of these receptors remain largely unknown. Here, we identify the GPI-linked protein Semaphorin-7A (CD108) as an erythrocyte receptor for the P. falciparum merozoite-specific TRAP homolog (MTRAP) by using a systematic screening approach designed to detect extracellular protein interactions. The specificity of the interaction was demonstrated by showing that binding was saturable and by quantifying the equilibrium and kinetic biophysical binding parameters using surface plasmon resonance. We found that two MTRAP monomers interact via their tandem TSR domains with the Sema domains of a Semaphorin-7A homodimer. Known naturally-occurring polymorphisms in Semaphorin-7A did not quantitatively affect MTRAP binding nor did the presence of glycans on the receptor. Attempts to block the interaction during in vitro erythrocyte invasion assays using recombinant proteins and antibodies showed no significant inhibitory effect, suggesting the inaccessibility of the complex to proteinaceous blocking agents. These findings now provide important experimental evidence to support the model that parasite TRAP-family ligands interact with specific host receptors during cellular invasion.
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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.