Contributors: Écologie et biologie des interactions (EBI Poitiers ); Université de Poitiers = University of Poitiers (UP)-Centre National de la Recherche Scientifique (CNRS); Analyse d'images biologiques - Biological Image Analysis (BIA); Institut Pasteur Paris (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); Plateforme de Protéomique / Proteomics platform; Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio); Institut Pasteur Paris (IP)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur Paris (IP)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS); Institut Pasteur Paris (IP)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); Institut de pharmacologie et de biologie structurale (IPBS); Université Toulouse III - Paul Sabatier (UT3); Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS); Fédération de Recherche nationale ProFI (FR ProFI); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS); Biologie des Interactions Hôte-Parasite - Biology of Host-Parasite Interactions; Institut Pasteur Paris (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); This work was supported by following funders: the Agence Nationale de la Recherche (grant ANR-17-CE13–00001–01 “Amocyst”) to A.S.-L.; the Labex IBEID (grant ANR-10-LABX-62-IBEID) and France-BioImaging infrastructure (grant ANR-10-INBS-04) to J.-C.O.-M.; and the Proteomics French Infrastructure, Investments for the Future (grant ANR-10-INBS-08) to M.L.P. The Photonic BioImaging Platform of Institut Pasteur was supported by France BioImaging, Investments for the Future (grant ANR-10–INBS–04).; ANR-17-CE13-0001,AmoCyst,Démêler les voies de signalisation impliquées dans l'enkystement des amibes pathogènes(2017); ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010); ANR-10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010); ANR-10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010)
نبذة مختصرة : International audience ; Amoebae found in aquatic and terrestrial environments encompass various pathogenic species, including the parasite Entamoeba histolytica and the free-living Acanthamoeba castellanii. Both microorganisms pose significant threats to public health, capable of inducing life-threatening effects on humans. These amoebae exist in two cellular forms: trophozoites and cysts. The trophozoite stage is the form used for growth and reproduction while the cyst stage is the resistant and disseminating form. Cysts occur after cellular metabolism slowdown due to nutritional deprivation or the appearance of environmental conditions unfavourable to the amoebae’s growth and division. The initiation of encystation is accompanied by the activation of stress responses, and scarce data indicate that encystation shares factors and mechanisms identified in stress responses occurring in trophozoites exposed to toxic compounds derived from human immune defence. Although some “omics” analyses have explored how amoebae respond to diverse stresses, these studies remain limited and rarely report post-translational modifications that would provide knowledge on the molecular mechanisms underlying amoebae-specific stress responses. In this review, we discuss ubiquitin-like proteins associated with encystation and cell survival during oxidative damage. We aim to shed light on the signalling pathways involved in amoebic defence mechanisms, with a focus on their potential clinical implications against pathogenic amoebae, addressing the pressing need for effective therapies.
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