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A novel lipase with dual localisation in Trypanosoma brucei
| dc.rights.license | open | en_US |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | MONIC, S.G. | |
| dc.contributor.author | LAMY, A. | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | THONNUS, M. | |
| dc.contributor.author | BIZARRA-REBELO, T. | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | BRINGAUD, F. | |
| dc.contributor.author | SMITH, T. | |
| dc.contributor.author | FIGUEIREDO, L. | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | RIVIÈRE, L. | |
| dc.date.accessioned | 2023-05-12T11:30:20Z | |
| dc.date.available | 2023-05-12T11:30:20Z | |
| dc.date.issued | 2022-12 | |
| dc.identifier.issn | 2045-2322 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/182079 | |
| dc.description.abstractEn | Abstract Phospholipases are esterases involved in lipid catabolism. In pathogenic micro-organisms (bacteria, fungi, parasites) they often play a critical role in virulence and pathogenicity. A few phospholipases (PL) have been characterised so far at the gene and protein level in unicellular parasites including African trypanosomes (AT). They could play a role in different processes such as host–pathogen interaction, antigenic variation, intermediary metabolism. By mining the genome database of AT we found putative new phospholipase candidate genes and here we provided biochemical evidence that one of these has lipolytic activity. This protein has a unique non-canonical glycosome targeting signal responsible for its dual localisation in the cytosol and the peroxisomes-related organelles named glycosomes. We also show that this new phospholipase is excreted by these pathogens and that antibodies directed against this protein are generated during an experimental infection with T. brucei gambiense , a subspecies responsible for infection in humans. This feature makes this protein a possible tool for diagnosis. | |
| dc.description.sponsorship | Interactions métaboliques entre les adipocytes et les trypanosomes, un nouveau paradigme pour les trypanosomoses - ANR-19-CE15-0004 | en_US |
| dc.description.sponsorship | Voies métaboliques glycosomales non glycolytiques: nouvelles fonctions pour le développement et la virulence des trypanosomes - ANR-15-CE15-0025 | en_US |
| dc.description.sponsorship | Alliance française contre les maladies parasitaires - ANR-11-LABX-0024 | en_US |
| dc.language.iso | EN | en_US |
| dc.rights | Attribution 3.0 United States | * |
| dc.rights.uri | http://creativecommons.org/licenses/by/3.0/us/ | * |
| dc.title.en | A novel lipase with dual localisation in Trypanosoma brucei | |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1038/s41598-022-08546-w | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio] | en_US |
| bordeaux.journal | Scientific Reports | en_US |
| bordeaux.page | 4766 | en_US |
| bordeaux.volume | 12 | en_US |
| bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
| bordeaux.issue | 1 | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| bordeaux.import.source | hal | |
| hal.identifier | hal-03819070 | |
| hal.version | 1 | |
| hal.export | false | |
| workflow.import.source | hal | |
| dc.rights.cc | CC BY | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific%20Reports&rft.date=2022-12&rft.volume=12&rft.issue=1&rft.spage=4766&rft.epage=4766&rft.eissn=2045-2322&rft.issn=2045-2322&rft.au=MONIC,%20S.G.&LAMY,%20A.&THONNUS,%20M.&BIZARRA-REBELO,%20T.&BRINGAUD,%20F.&rft.genre=article |
