An apical membrane complex controls rhoptry exocytosis and invasion in Toxoplasma

التفاصيل البيبلوغرافية
العنوان: An apical membrane complex controls rhoptry exocytosis and invasion in Toxoplasma
المؤلفون: Sparvoli, Daniela, Delabre, Jason, Penarete-Vargas, Diana Marcela, Mageswaran, Shrawan Kumar, Tsypin, Lev M., Heckendorn, Justine, Theveny, Liam, Maynadier, Marjorie, Cova, Marta Mendonça, Berry-Sterkers, Laurence, Guérin, Amandine, Dubremetz, Jean-François, Urbach, Serge, Striepen, Boris, Turkewitz, Aaron P., Chang, Yi-Wei, Lebrun, Maryse
سنة النشر: 2022
المجموعة: Caltech Authors (California Institute of Technology)
مصطلحات موضوعية: Apicomplexa, Ciliates, Plasmodium, Toxoplasma, Rhoptry, exocytosis, invasion, CRMP, Alveolata, signaling
الوصف: Apicomplexan parasites possess secretory organelles called rhoptries that undergo regulated exocytosis upon contact with the host. This process is essential for the parasitic lifestyle of these pathogens and relies on an exocytic machinery sharing structural features and molecular components with free-living ciliates. Here, we performed a Tetrahymena-based transcriptomic screen to uncover novel exocytic factors in Ciliata and Apicomplexa. We identified membrane-bound proteins, named CRMPs, forming part of a large complex essential for rhoptry secretion and invasion in Toxoplasma. In contrast to previously described rhoptry exocytic factors, TgCRMPs are not required for the assembly of the rhoptry secretion machinery and only transiently associated with the exocytic site - prior to invasion. CRMPs and their partners contain putative host cell-binding domains, and CRMPa shares similarity to GPCR proteins. We propose that the CRMP complex acts as host-molecular sensor to ensure that rhoptry exocytosis occurs when the parasite contacts the host cell. ; The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. We thank Sebastian Lourido for the pU6-Universal plasmid, Dominique Soldati-Favre for providing the anti-ARM (ARO) antibodies and pLinker-2xTy-DHFR plasmid, Nicolas Dos Santos Pacheco for helping in setting up the Ultrastructure Expansion Microscopy, Anita Koshy for the toxofilin-Cre plasmid and Helen Blau's lab for the Cre reporter DSred cell line. We thank Veronique Richard and Frank Godiard of the MEA platform, University of Montpellier for their assistance with electron microscopy and Pilar Ruga Fahy of the Pôle Facultaire de Microscopie Ultrastructurale, in Geneva for preparation of freeze-fracture replicas. We are also grateful to Elodie Jublanc, Vicky Diakou and the imaging facility MRI at the University of Montpellier, part of the national infrastructure France-BioImaging supported by the French National Research Agency ...
نوع الوثيقة: report
اللغة: unknown
العلاقة: https://doi.org/10.1101/2022.02.25.481937Test; oai:authors.library.caltech.edu:68nav-tag53; eprintid:113625; resolverid:CaltechAUTHORS:20220228-619488000
DOI: 10.1101/2022.02.25.481937
الإتاحة: https://doi.org/10.1101/2022.02.25.481937Test
حقوق: info:eu-repo/semantics/openAccess ; Other
رقم الانضمام: edsbas.111DB48B
قاعدة البيانات: BASE