ArticleMolecular & cellular proteomics : MCP2011
Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motility.
Article in Molecular & cellular proteomics : MCP, 2011. 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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Characterization and functional analysis ofmBio · 2024Article
- N-acetylglucosamine supplementation fails to bypass the critical acetylation of glucosamine-6-phosphate required for Toxoplasma gondii replication and invasion.PLoS pathogens · 2024Article
- Glycosylation Analysis of Feline Small Intestine FollowingAnimals : an open access journal from MDPI · 2022Article
- Eimeria falciformis secretes extracellular vesicles to modulate proinflammatory response during interaction with mouse intestinal epithelial cells.Parasites & vectors · 2022Article
- Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Genomic reconstruction and features of glycosylation pathways in the apicomplexanFrontiers in molecular biosciences · 2022Review
- CRISPR/Cas9 and glycomics tools forThe Journal of biological chemistry · 2019Article
- Toxoplasma gondii tachyzoite-extract acts as a potent immunomodulator against allergic sensitization and airway inflammation.Scientific reports · 2017Article
- Asparagine-Linked Glycans ofMolecular & cellular proteomics : MCP · 2017Article
- Extracellular Toxoplasma gondii tachyzoites metabolize and incorporate unnatural sugars into cellular proteins.Microbes and infection · 2016Article
- Gliding Associated Proteins Play Essential Roles during the Formation of the Inner Membrane Complex of Toxoplasma gondii.PLoS pathogens · 2016Article
- Identification of Novel O-Linked Glycosylated Toxoplasma Proteins by Vicia villosa Lectin Chromatography.PloS one · 2016Article
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- The inner membrane complex through development of Toxoplasma gondii and Plasmodium.Cellular microbiology · 2014Review
- Genetic basis for phenotypic differences between different Toxoplasma gondii type I strains.BMC genomics · 2013Article
- SAG2A protein from Toxoplasma gondii interacts with both innate and adaptive immune compartments of infected hosts.Parasites & vectors · 2013Article
- Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation.PloS one · 2012Article
Corrections and comments
- Erratum issuedDilezitoko Ayali, Tchilabalo [corrected to Dilezitoko Alayi, Tchilabalo]
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxoplasma gondii motility, which is essential for host cell entry, migration through host tissues, and invasion, is a unique form of actin-dependent gliding. It is powered by a motor complex mainly composed of myosin heavy chain A, myosin light chain 1, gliding associated proteins GAP45, and GAP50, the only integral membrane anchor so far described. In the present study, we have combined glycomic and proteomic approaches to demonstrate that all three potential N-glycosylated sites of GAP50 are occupied by unusual N-glycan structures that are rarely found on mature mammalian glycoproteins. Using site-directed mutagenesis, we show that N-glycosylation is a prerequisite for GAP50 transport from the endoplasmic reticulum to the Golgi apparatus and for its subsequent delivery into the inner complex membrane. Assembly of key partners into the gliding complex, and parasite motility are severely impaired in the unglycosylated GAP50 mutants. Furthermore, comparative affinity purification using N-glycosylated and unglycosylated GAP50 as bait identified three novel hypothetical proteins including the recently described gliding associated protein GAP40, and we demonstrate that N-glycans are required for efficient binding to gliding partners. Collectively, these results provide the first detailed analyses of T. gondii N-glycosylation functions that are vital for parasite motility and host cell entry.
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