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弓形虫中非常规的内体样区室和逆向转运复合物决定寄生虫的完整性和宿主感染。

Unconventional endosome-like compartment and retromer complex in Toxoplasma gondii govern parasite integrity and host infection.

作者信息

Sangaré Lamba Omar, Alayi Tchilabalo Dilezitoko, Westermann Benoit, Hovasse Agnes, Sindikubwabo Fabien, Callebaut Isabelle, Werkmeister Elisabeth, Lafont Frank, Slomianny Christian, Hakimi Mohamed-Ali, Van Dorsselaer Alain, Schaeffer-Reiss Christine, Tomavo Stanislas

机构信息

Center for Infection and Immunity of Lille, INSERM U 1019, CNRS UMR 8204, Institut Pasteur de Lille, Université de Lille, 59000 Lille, France.

Laboratory of Bio-Organic Mass Spectrometry, IPHC, CNRS UMR 7178, Université de Strasbourg, 67087 Strasbourg, France.

出版信息

Nat Commun. 2016 Apr 11;7:11191. doi: 10.1038/ncomms11191.

DOI:10.1038/ncomms11191
PMID:27064065
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4831018/
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.

摘要

膜运输途径在顶复门寄生虫中起着关键作用，顶复门是一类原生动物寄生虫，在全球范围内可引发危及生命的疾病。在此，我们报道了刚地弓形虫中首个逆向转运蛋白相互作用组。该逆向转运蛋白复合物包括一个三聚体Vps35-Vps26-Vps29核心复合物，它作为内体样区室和寄生虫特异性蛋白的枢纽。对TgVps35进行条件性敲除表明，逆向转运蛋白复合物对于分泌细胞器的生物发生以及维持寄生虫形态至关重要。我们将TgHP12鉴定为一种与寄生虫特异性和逆向转运蛋白相关的蛋白，其功能与分泌细胞器形成无关。此外，主要易化子超家族同源物TgHP03是一种多次跨膜的配体跨膜转运蛋白，通过逆向转运蛋白介导的内吞再循环维持在寄生虫膜上。因此我们的研究结果表明，进化上保守的蛋白和非常规蛋白在刚地弓形虫中协同作用，通过控制对寄生虫完整性和宿主感染至关重要的逆向转运来发挥作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/85a1192e7314/ncomms11191-f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/285f3a165575/ncomms11191-f1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/92bbb95bfce2/ncomms11191-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/14596476e2c6/ncomms11191-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/32dd5d7f8507/ncomms11191-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/ae60b0cea40b/ncomms11191-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/f4f5a53770d9/ncomms11191-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/cc699a729835/ncomms11191-f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/85a1192e7314/ncomms11191-f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/285f3a165575/ncomms11191-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/c70b56aff12d/ncomms11191-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/ea77bab322b5/ncomms11191-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/92bbb95bfce2/ncomms11191-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/14596476e2c6/ncomms11191-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/32dd5d7f8507/ncomms11191-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/ae60b0cea40b/ncomms11191-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/f4f5a53770d9/ncomms11191-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/cc699a729835/ncomms11191-f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6bba/4831018/85a1192e7314/ncomms11191-f10.jpg

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