Plasmodium berghei leucine-rich repeat ...
Document type :
Article dans une revue scientifique: Article original
DOI :
Title :
Plasmodium berghei leucine-rich repeat protein 1 downregulates protein phosphatase 1 activity and is required for efficient oocyst development
Author(s) :
Fréville, Aline [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Gnangnon, Bénédicte [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Tremp, Annie [Auteur]
London School of Hygiene and Tropical Medicine [LSHTM]
De Witte, Caroline [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Cailliau, Katia [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Martoriati, Alain [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Aliouat, El Moukthar [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Fernandes, Priyanka [Auteur]
Centre d'Immunologie et des Maladies Infectieuses [CIMI]
Chhuon, Cerina [Auteur]
Plateforme Protéomique Necker [SFR Necker] [PPN - 3P5]
Silvie, Olivier [Auteur]
Centre d'Immunologie et des Maladies Infectieuses [CIMI]
Marion, Sabrina [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Guerrera, Ida Chiara [Auteur]
Plateforme Protéomique Necker [SFR Necker] [PPN - 3P5]
Dessens, Johannes [Auteur]
London School of Hygiene and Tropical Medicine [LSHTM]
Pierrot, Christine [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Khalife, Jamal [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Gnangnon, Bénédicte [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Tremp, Annie [Auteur]
London School of Hygiene and Tropical Medicine [LSHTM]
De Witte, Caroline [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Cailliau, Katia [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Martoriati, Alain [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Aliouat, El Moukthar [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Fernandes, Priyanka [Auteur]
Centre d'Immunologie et des Maladies Infectieuses [CIMI]
Chhuon, Cerina [Auteur]
Plateforme Protéomique Necker [SFR Necker] [PPN - 3P5]
Silvie, Olivier [Auteur]
Centre d'Immunologie et des Maladies Infectieuses [CIMI]
Marion, Sabrina [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Guerrera, Ida Chiara [Auteur]
Plateforme Protéomique Necker [SFR Necker] [PPN - 3P5]
Dessens, Johannes [Auteur]
London School of Hygiene and Tropical Medicine [LSHTM]
Pierrot, Christine [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Khalife, Jamal [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Journal title :
Open biology
Open biology
Open biology
Pages :
220015
Publisher :
Royal Society
Publication date :
2022
English keyword(s) :
eucine-rich repeat protein 1
SDS22
protein phosphatase 1
PP1
inhibitor 3
SDS22
protein phosphatase 1
PP1
inhibitor 3
HAL domain(s) :
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Parasitologie
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Sciences du Vivant [q-bio]/Biologie du développement
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Sciences du Vivant [q-bio]/Biologie du développement
English abstract : [en]
Protein phosphatase 1 (PP1) is a key enzyme for Plasmodium development. However, the detailed mechanisms underlying its regulation remain to be deciphered. Here, we report the functional characterization of the Plasmodium ...
Show more >Protein phosphatase 1 (PP1) is a key enzyme for Plasmodium development. However, the detailed mechanisms underlying its regulation remain to be deciphered. Here, we report the functional characterization of the Plasmodium berghei leucine-rich repeat protein 1 (PbLRR1), an orthologue of SDS22, one of the most ancient and conserved PP1 interactors. Our study shows that PbLRR1 is expressed during intra-erythrocytic development of the parasite, and up to the zygote stage in mosquitoes. PbLRR1 can be found in complex with PbPP1 in both asexual and sexual stages and inhibits its phosphatase activity. Genetic analysis demonstrates that PbLRR1 depletion adversely affects the development of oocysts. PbLRR1 interactome analysis associated with phospho-proteomics studies identifies several novel putative PbLRR1/PbPP1 partners. Some of these partners have previously been characterized as essential for the parasite sexual development. Interestingly, and for the first time, Inhibitor 3 (I3), a well-known and direct interactant of Plasmodium PP1, was found to be drastically hypophosphorylated in PbLRR1-depleted parasites. These data, along with the detection of I3 with PP1 in the LRR1 interactome, strongly suggest that the phosphorylation status of PbI3 is under the control of the PP1–LRR1 complex and could contribute (in)directly to oocyst development. This study provides new insights into previously unrecognized PbPP1 fine regulation of Plasmodium oocyst development through its interaction with PbLRR1.Show less >
Show more >Protein phosphatase 1 (PP1) is a key enzyme for Plasmodium development. However, the detailed mechanisms underlying its regulation remain to be deciphered. Here, we report the functional characterization of the Plasmodium berghei leucine-rich repeat protein 1 (PbLRR1), an orthologue of SDS22, one of the most ancient and conserved PP1 interactors. Our study shows that PbLRR1 is expressed during intra-erythrocytic development of the parasite, and up to the zygote stage in mosquitoes. PbLRR1 can be found in complex with PbPP1 in both asexual and sexual stages and inhibits its phosphatase activity. Genetic analysis demonstrates that PbLRR1 depletion adversely affects the development of oocysts. PbLRR1 interactome analysis associated with phospho-proteomics studies identifies several novel putative PbLRR1/PbPP1 partners. Some of these partners have previously been characterized as essential for the parasite sexual development. Interestingly, and for the first time, Inhibitor 3 (I3), a well-known and direct interactant of Plasmodium PP1, was found to be drastically hypophosphorylated in PbLRR1-depleted parasites. These data, along with the detection of I3 with PP1 in the LRR1 interactome, strongly suggest that the phosphorylation status of PbI3 is under the control of the PP1–LRR1 complex and could contribute (in)directly to oocyst development. This study provides new insights into previously unrecognized PbPP1 fine regulation of Plasmodium oocyst development through its interaction with PbLRR1.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Source :
Files
- https://hal.archives-ouvertes.fr/hal-03798409/document
- Open access
- Access the document
- https://hal.archives-ouvertes.fr/hal-03798409/document
- Open access
- Access the document
- document
- Open access
- Access the document
- rsob-JK.pdf
- Open access
- Access the document
- document
- Open access
- Access the document
- rsob-JK.pdf
- Open access
- Access the document