ArticleThe Journal of biological chemistry2012
Galactose recognition by the apicomplexan parasite Toxoplasma gondii.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 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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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.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
- HarnessingAnnals of medicine · 2026Review
- Clustering of host N-glycans by the microneme MIC1/4/6 complex licenses Toxoplasma rhoptry discharge.The EMBO journal · 2026Article
- Surface antigen SAG1 mediatesInfection and immunity · 2025Article
- Recombinant Microneme Proteins MIC1 and MIC4 fromPathogens (Basel, Switzerland) · 2025Article
- Dynamic RNA profiles in the small intestinal epithelia of cats after Toxoplasma gondii infection.Infectious diseases of poverty · 2023Article
- Conservation, abundance, glycosylation profile, and localization of the TSP protein family in Cryptosporidium parvum.The Journal of biological chemistry · 2023Article
- Dominique Soldati-Favre: BringingFrontiers in cellular and infection microbiology · 2022Article
- Global transcriptome landscape of the rabbit protozoan parasite Eimeria stiedae.Parasites & vectors · 2021Article
- Microneme Proteins 1 and 4 FromFrontiers in immunology · 2021Article
- The Potential Contribution of ABO, Lewis and Secretor Histo-Blood Group Carbohydrates in Infection byFrontiers in cellular and infection microbiology · 2021Article
- Diverse Roles of TgMIC1/4/6 in theFrontiers in microbiology · 2021Review
- Development of multiepitope subunit protein vaccines againstNAR genomics and bioinformatics · 2020Article
- Receptor Heterodimerization and Co-Receptor Engagement in TLR2 Activation Induced by MIC1 and MIC4 fromInternational journal of molecular sciences · 2019Article
- The lectin-specific activity of Toxoplasma gondii microneme proteins 1 and 4 binds Toll-like receptor 2 and 4 N-glycans to regulate innate immune priming.PLoS pathogens · 2019Article
- Secretory Microneme Proteins Induce T-Cell Recall Responses in Mice Chronically Infected with Toxoplasma gondii.mSphere · 2019Article
- How does Toxoplama gondii invade host cells?The Journal of veterinary medical science · 2018Review
- Conformations of the type-1 lacto-N-biose I unit in protein complex structures.Acta crystallographica. Section F, Structural biology communications · 2018Review
- Immunomolecular Characterization of MIC-1, a Novel Antigen in Babesia bigemina, Which Contains Conserved and Immunodominant B-Cell Epitopes that Induce Neutralizing Antibodies.Veterinary sciences · 2018Article
- Twenty-six circulating antigens and two novel diagnostic candidate molecules identified in the serum of canines with experimental acute toxoplasmosis.Parasites & vectors · 2016Article
- Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2.The Journal of biological chemistry · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
17 authors at 5 institutions in 3 countries.
Funding
Abstract
Toxosplasma gondii is the model parasite of the phylum Apicomplexa, which contains numerous obligate intracellular parasites of medical and veterinary importance, including Eimeria, Sarcocystis, Cryptosporidium, Cyclospora, and Plasmodium species. Members of this phylum actively enter host cells by a multistep process with the help of microneme protein (MIC) complexes that play important roles in motility, host cell attachment, moving junction formation, and invasion. T. gondii (Tg)MIC1-4-6 complex is the most extensively investigated microneme complex, which contributes to host cell recognition and attachment via the action of TgMIC1, a sialic acid-binding adhesin. Here, we report the structure of TgMIC4 and reveal its carbohydrate-binding specificity to a variety of galactose-containing carbohydrate ligands. The lectin is composed of six apple domains in which the fifth domain displays a potent galactose-binding activity, and which is cleaved from the complex during parasite invasion. We propose that galactose recognition by TgMIC4 may compromise host protection from galectin-mediated activation of the host immune system.
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What OpenQuestion holds
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.