Unconventional endosome-like compartment and retromer complex in Toxoplasma gondii govern parasite integrity and host infection
Lamba Omar Sangaré,
Tchilabalo Dilezitoko Alayi,
Benoit Westermann,
Agnes Hovasse,
Fabien Sindikubwabo,
Isabelle Callebaut,
Elisabeth Werkmeister,
Frank Lafont,
Christian Slomianny,
Mohamed-Ali Hakimi,
Alain Van Dorsselaer,
Christine Schaeffer-Reiss and
Stanislas Tomavo ()
Additional contact information
Lamba Omar Sangaré: Center for Infection and Immunity of Lille, INSERM U 1019, CNRS UMR 8204, Institut Pasteur de Lille, Université de Lille
Tchilabalo Dilezitoko Alayi: Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg
Benoit Westermann: Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg
Agnes Hovasse: Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg
Fabien Sindikubwabo: CNRS UMR5163, LAPM, Université Joseph Fourier
Isabelle Callebaut: CNRS UMR7590, Sorbonne Universités, Université Pierre et Marie Curie-Paris 6, MNHN, IRD-IUC
Elisabeth Werkmeister: Bioimaging Platform, IBL, CNRS, Université de Lille
Frank Lafont: Bioimaging Platform, IBL, CNRS, Université de Lille
Christian Slomianny: Laboratory of Cell Physiology, INSERM U 1003, Université de Lille
Mohamed-Ali Hakimi: CNRS UMR5163, LAPM, Université Joseph Fourier
Alain Van Dorsselaer: Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg
Christine Schaeffer-Reiss: Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg
Stanislas Tomavo: Center for Infection and Immunity of Lille, INSERM U 1019, CNRS UMR 8204, Institut Pasteur de Lille, Université de Lille
Nature Communications, 2016, vol. 7, issue 1, 1-14
Abstract:
Abstract Membrane trafficking pathways play critical roles in Apicomplexa, a phylum of protozoan parasites that cause life-threatening diseases worldwide. Here we report the first retromer-trafficking interactome in Toxoplasma gondii. This retromer complex includes a trimer Vps35–Vps26–Vps29 core complex that serves as a hub for the endosome-like compartment and parasite-specific proteins. Conditional ablation of TgVps35 reveals that the retromer complex is crucial for the biogenesis of secretory organelles and for maintaining parasite morphology. We identify TgHP12 as a parasite-specific and retromer-associated protein with functions unrelated to secretory organelle formation. Furthermore, the major facilitator superfamily homologue named TgHP03, which is a multiple spanning and ligand transmembrane transporter, is maintained at the parasite membrane by retromer-mediated endocytic recycling. Thus, our findings highlight that both evolutionarily conserved and unconventional proteins act in concert in T. gondii by controlling retrograde transport that is essential for parasite integrity and host infection.
Date: 2016
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/ncomms11191 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11191
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms11191
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().