ArticleMolecular microbiology2010
Toxoplasma gondii transmembrane microneme proteins and their modular design.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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.
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Who cites it
41 citing papers in PubMed, 79 citations in OpenAlex.
- HarnessingAnnals of medicine · 2026Review
- Toxoplasma FER1 is a versatile and dynamic mediator of differential microneme trafficking and microneme exocytosis.Scientific reports · 2024Article
- ToxoNet: A high confidence map of protein-protein interactions in Toxoplasma gondii.PLoS computational biology · 2024Article
- A conserved complex of microneme proteins mediates rhoptry discharge in Toxoplasma.The EMBO journal · 2023Article
- Tryptophan C-mannosylation is critical for Plasmodium falciparum transmission.Nature communications · 2022Article
- Dominique Soldati-Favre: BringingFrontiers in cellular and infection microbiology · 2022Article
- Functional Characterization of the Thrombospondin-Related Paralogous Proteins Rhoptry Discharge Factors 1 and 2 Unveils Phenotypic Plasticity inFrontiers in microbiology · 2022Article
- Ferlins and TgDOC2 inLife (Basel, Switzerland) · 2021Article
- Protective Immunity Induced by TgMIC5 and TgMIC16 DNA Vaccines Against Toxoplasmosis.Frontiers in cellular and infection microbiology · 2021Article
- Diverse Roles of TgMIC1/4/6 in theFrontiers in microbiology · 2021Review
- Multi-omics analysis delineates the distinct functions of sub-cellular acetyl-CoA pools in Toxoplasma gondii.BMC biology · 2020Article
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- Interplay BetweenFrontiers in cellular and infection microbiology · 2019Review
- Discovery of Plasmodium (M)TRAP-Aldolase Interaction Stabilizers Interfering with Sporozoite Motility and Invasion.ACS infectious diseases · 2018Article
- Myosin-dependent cell-cell communication controls synchronicity of division in acute and chronic stages of Toxoplasma gondii.Nature communications · 2017Article
- Cdk7 mediates RPB1-driven mRNA synthesis in Toxoplasma gondii.Scientific reports · 2016Article
- MIC16 gene represents a potential novel genetic marker for population genetic studies of Toxoplasma gondii.BMC microbiology · 2016Article
- The mechanics of malaria parasite invasion of the human erythrocyte - towards a reassessment of the host cell contribution.Cellular microbiology · 2016Review
- Identification and characterization of a microneme protein (NcMIC6) in Neospora caninum.Parasitology research · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Host cell invasion by the Apicomplexa critically relies on regulated secretion of transmembrane micronemal proteins (TM-MICs). Toxoplasma gondii possesses functionally non-redundant MIC complexes that participate in gliding motility, host cell attachment, moving junction formation, rhoptry secretion and invasion. The TM-MICs are released onto the parasite's surface as complexes capable of interacting with host cell receptors. Additionally, TgMIC2 simultaneously connects to the actomyosin system via binding to aldolase. During invasion these adhesive complexes are shed from the surface notably via intramembrane cleavage of the TM-MICs by a rhomboid protease. Some TM-MICs act as escorters and assure trafficking of the complexes to the micronemes. We have investigated the properties of TgMIC6, TgMIC8, TgMIC8.2, TgAMA1 and the new micronemal protein TgMIC16 with respect to interaction with aldolase, susceptibility to rhomboid cleavage and presence of trafficking signals. We conclude that several TM-MICs lack targeting information within their C-terminal domains, indicating that trafficking depends on yet unidentified proteins interacting with their ectodomains. Most TM-MICs serve as substrates for a rhomboid protease and some of them are able to bind to aldolase. We also show that the residues responsible for binding to aldolase are essential for TgAMA1 but dispensable for TgMIC6 function during 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.