ArticleTraffic (Copenhagen, Denmark)2013
A HT/PEXEL motif in Toxoplasma dense granule proteins is a signal for protein cleavage but not export into the host cell.
Article in Traffic (Copenhagen, Denmark), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Article
- Article
- Subversion from Within and Without: Effector Molecule Transfer from Obligate Intracellular Apicomplexan Parasites to Human Host Cells.Results and problems in cell differentiation · 2024Review
- Advances in understanding red blood cell modifications by Babesia.PLoS pathogens · 2022Review
- Unique Endomembrane Systems and Virulence in Pathogenic Protozoa.Life (Basel, Switzerland) · 2021Review
- Non-ribosomal insights into ribosomal P2 protein in Plasmodium falciparum-infected erythrocytes.MicrobiologyOpen · 2021Article
- Applying Machine Learning to Predict the Exportome of Bovine and CaninePathogens (Basel, Switzerland) · 2021Article
- A Family of Toxoplasma gondii Genes Related to GRA12 Regulate Cyst Burdens and Cyst Reactivation.mSphere · 2021Article
- Novel Babesia bovis exported proteins that modify properties of infected red blood cells.PLoS pathogens · 2020Article
- Review
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites.Microorganisms · 2020Review
- Proximity biotinylation reveals novel secreted dense granule proteins of Toxoplasma gondii bradyzoites.PloS one · 2020Article
- Translocation of effector proteins into host cells by Toxoplasma gondii.Current opinion in microbiology · 2019Review
- The GRA15 protein fromThe Journal of biological chemistry · 2019Article
- Article
- TheBiology open · 2019Article
- Characterization of aeLife · 2018Article
- Functional Characterization of Dense Granule Proteins inFrontiers in cellular and infection microbiology · 2018Article
- Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Apicomplexan parasites, such as Toxoplasma gondii and Plasmodium, secrete proteins for attachment, invasion and modulation of their host cells. The host targeting (HT), also known as the Plasmodium export element (PEXEL), directs Plasmodium proteins into erythrocytes to remodel the host cell and establish infection. Bioinformatic analysis of Toxoplasma revealed a HT/PEXEL-like motif at the N-terminus of several hypothetical unknown and dense granule proteins. Hemagglutinin-tagged versions of these uncharacterized proteins show co-localization with dense granule proteins found on the parasitophorous vacuole membrane (PVM). In contrast to Plasmodium, these Toxoplasma HT/PEXEL containing proteins are not exported into the host cell. Site directed mutagenesis of the Toxoplasma HT/PEXEL motif, RxLxD/E, shows that the arginine and leucine residues are permissible for protein cleavage. Mutations within the HT/PEXEL motif that prevent protein cleavage still allow for targeting to the PV but the proteins have a reduced association with the PVM. Addition of a Myc tag before and after the cleavage site shows that processed HT/PEXEL protein has increased PVM association. These findings suggest that while Toxoplasma and Plasmodium share similar HT/PEXEL motifs, Toxoplasma HT/PEXEL containing proteins interact with but do not cross the PVM.
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