A novel lipase with dual localisation in Trypanosoma brucei

© 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/.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.Experiment 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.