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A novel lipase with dual localisation in Trypanosoma brucei

dc.contributor.authorMonic, S. G.
dc.contributor.authorLamy, A.
dc.contributor.authorThonnus, M.
dc.contributor.authorBizarra-Rebelo, T.
dc.contributor.authorBringaud, F.
dc.contributor.authorSmith, T. K.
dc.contributor.authorFigueiredo, Luisa M.
dc.contributor.authorRivière, L.
dc.date.accessioned2022-03-28T15:52:08Z
dc.date.available2022-03-28T15:52:08Z
dc.date.issued2022
dc.description© The Author(s) 2022. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.pt_PT
dc.description.abstractPhospholipases 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.pt_PT
dc.description.sponsorshipExperiment costs were supported by Université de Bordeaux (https://www.u-bordeaux.fr), CNRS (https://www.cnrs.fr) and the Agence Nationale de la Recherche through the grants GLYCONOV (grant number ANR-15-CE-15-0025-01) and ADIPOTRYP (grant number ANR19-CE15-0004-01). This work was also funded by the Laboratoire d’Excellence (LabEx) “French Parasitology Alliance For Health Care” (ANR-11-LABX-0024-PARAFRAP, https://labex-parafrap.fr). This work was also partially supported by the European Research Council (FatTryp, ref. 771714) and by Fundacao para a Ciencia e Tecnologia (CEECIND/03322/2018) awarded to LMF.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationSci Rep. 2022 Mar 19;12(1):4766pt_PT
dc.identifier.doi10.1038/s41598-022-08546-wpt_PT
dc.identifier.eissn2045-2322
dc.identifier.urihttp://hdl.handle.net/10451/52028
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherSpringer Naturept_PT
dc.relationCEECIND/03322/2018pt_PT
dc.relationExploring the hidden life of African trypanosomes: parasite fat tropism and implications for disease
dc.relation.publisherversionhttps://www.nature.com/srep/pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleA novel lipase with dual localisation in Trypanosoma bruceipt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleExploring the hidden life of African trypanosomes: parasite fat tropism and implications for disease
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/771714/EU
oaire.citation.issue1pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume12pt_PT
oaire.fundingStreamH2020
person.familyNameFigueiredo
person.givenNameLuisa M
person.identifier.ciencia-id421C-420D-E7BD
person.identifier.orcid0000-0002-5752-6586
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication996632d8-b4b7-45ab-903f-aec092718a0d
relation.isAuthorOfPublication.latestForDiscovery996632d8-b4b7-45ab-903f-aec092718a0d
relation.isProjectOfPublicationa129aa83-6d3e-4f27-a015-1842a6bd7ea0
relation.isProjectOfPublication.latestForDiscoverya129aa83-6d3e-4f27-a015-1842a6bd7ea0

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