Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii

Most intracellular pathogens replicate in a vacuole to avoid the defense system of the host. A few pathogens recruit host mitochondria around those vacuoles, but the molecules responsible for mitochondrial recruitment remain unidentified. It is only in the apicomplexan parasite Toxoplasma gondii, th...

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Autores principales:	Junpei Fukumoto, Takaya Sakura, Ryuma Matsubara, Michiru Tahara, Motomichi Matsuzaki, Kisaburo Nagamune
Formato:	article
Lenguaje:	EN
Publicado:	The Company of Biologists 2021
Materias:	toxoplasma gondii quantitative proteomics rop39 host mitochondrial recruitment Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/01be01b41e244ccfb101e6f9866f2494
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spelling	oai:doaj.org-article:01be01b41e244ccfb101e6f9866f24942021-11-28T16:01:31ZRhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii2046-639010.1242/bio.058988https://doaj.org/article/01be01b41e244ccfb101e6f9866f24942021-09-01T00:00:00Zhttp://bio.biologists.org/content/10/9/bio058988https://doaj.org/toc/2046-6390Most intracellular pathogens replicate in a vacuole to avoid the defense system of the host. A few pathogens recruit host mitochondria around those vacuoles, but the molecules responsible for mitochondrial recruitment remain unidentified. It is only in the apicomplexan parasite Toxoplasma gondii, that mitochondrial association factor 1b (MAF1b) has been identified as an association factor for host mitochondria. Here, we show that rhoptry kinase family protein 39 (ROP39) induces host mitochondrial recruitment in T. gondii. We found that the abundance of ROP39 was increased on host mitochondria extracted from human foreskin fibroblasts (HFFs) infected with T. gondii. ROP39 expressed exogenously in HFFs localized on host mitochondria, indicating that it has the potential to bind to host mitochondria without assistance from other parasite factors. Confocal microscopy revealed that ROP39 colocalized with host mitochondria on the membrane of parasitophorous vacuoles, in which the parasites reside. Moreover, we observed about a 10% reduction in the level of mitochondrial association in rop39-knockout parasites compared with a parental strain.Junpei FukumotoTakaya SakuraRyuma MatsubaraMichiru TaharaMotomichi MatsuzakiKisaburo NagamuneThe Company of Biologistsarticletoxoplasma gondiiquantitative proteomicsrop39host mitochondrial recruitmentScienceQBiology (General)QH301-705.5ENBiology Open, Vol 10, Iss 9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	toxoplasma gondii quantitative proteomics rop39 host mitochondrial recruitment Science Q Biology (General) QH301-705.5
spellingShingle	toxoplasma gondii quantitative proteomics rop39 host mitochondrial recruitment Science Q Biology (General) QH301-705.5 Junpei Fukumoto Takaya Sakura Ryuma Matsubara Michiru Tahara Motomichi Matsuzaki Kisaburo Nagamune Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
description	Most intracellular pathogens replicate in a vacuole to avoid the defense system of the host. A few pathogens recruit host mitochondria around those vacuoles, but the molecules responsible for mitochondrial recruitment remain unidentified. It is only in the apicomplexan parasite Toxoplasma gondii, that mitochondrial association factor 1b (MAF1b) has been identified as an association factor for host mitochondria. Here, we show that rhoptry kinase family protein 39 (ROP39) induces host mitochondrial recruitment in T. gondii. We found that the abundance of ROP39 was increased on host mitochondria extracted from human foreskin fibroblasts (HFFs) infected with T. gondii. ROP39 expressed exogenously in HFFs localized on host mitochondria, indicating that it has the potential to bind to host mitochondria without assistance from other parasite factors. Confocal microscopy revealed that ROP39 colocalized with host mitochondria on the membrane of parasitophorous vacuoles, in which the parasites reside. Moreover, we observed about a 10% reduction in the level of mitochondrial association in rop39-knockout parasites compared with a parental strain.
format	article
author	Junpei Fukumoto Takaya Sakura Ryuma Matsubara Michiru Tahara Motomichi Matsuzaki Kisaburo Nagamune
author_facet	Junpei Fukumoto Takaya Sakura Ryuma Matsubara Michiru Tahara Motomichi Matsuzaki Kisaburo Nagamune
author_sort	Junpei Fukumoto
title	Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
title_short	Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
title_full	Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
title_fullStr	Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
title_full_unstemmed	Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii
title_sort	rhoptry kinase protein 39 (rop39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of toxoplasma gondii
publisher	The Company of Biologists
publishDate	2021
url	https://doaj.org/article/01be01b41e244ccfb101e6f9866f2494
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Rhoptry kinase protein 39 (ROP39) is a novel factor that recruits host mitochondria to the parasitophorous vacuole of Toxoplasma gondii

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