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oai:figshare.com:article/34073853 2026-10-05T17:53:30Z category_4 category_915 category_7 category_8 category_12 category_272 category_39 category_46 category_734 category_132 category_135 portal_5 item_type_3 month_year_10_2026

pone.0356818.t001 - <p> </p> Daniel Martel (25317285) Olivier Leclercq (84066) Florent Dingli (174202) Victor Laigle (12005942) Nawal Hajj Sleiman (25317288) Damarys Loew (85777) Gerald F. Späth (8948342) Najma Rachidi (524193) Biochemistry Physical Sciences not elsewhere classified Medicine Microbiology Cell Biology Environmental Sciences not elsewhere classified Ecology Immunology Biological Sciences not elsewhere classified Infectious Diseases Computational Biology various cellular structures dynamic localization pattern providing potential targets potential interacting partners associated proteins across four host proteins potential dual function interacting partners within host cell (< using proteomic analysis identified 230 l potential importance dual functions analysis revealed work provides vitro </ ubiquitous presence trans </ study investigates study highlights regulating intracellular purine biosynthesis pathogen interactions parasitic organisms parasite (< leishmania </ key player immune response findings may evolutionary conservation confocal microscopy comprehensive map cis </ causative agent broader implications broad spectrum basal body >), positioning <div><p><i>Leishmania</i> CK1.2 (L-CK1.2) is a serine/threonine protein kinase essential for the survival of the protozoan parasite <i>Leishmania</i>, the causative agent of leishmaniasis. This study investigates the dynamic localization pattern of L-CK1.2 and the broad spectrum of its interacting partners within the parasite. Using proteomic analysis and confocal microscopy, we identified 230 L-CK1.2-associated proteins across the major parasite life stages. This analysis revealed the ubiquitous presence of L-CK1.2 in various cellular structures, including the cytoskeleton, basal body, and flagellum. Using an <i>in vitro</i> system, sixty-four host proteins, involved in critical host biological processes such as immune response, apoptosis, and purine biosynthesis, were identified as potential interacting partners of L-CK1.2. These processes are known to be regulated by <i>Leishmania</i> during infection. The study highlights the potential dual function of L-CK1.2, in the parasite (<i>cis</i>) and within the host cell (<i>trans</i>), positioning this kinase as a key player in host-pathogen interactions. This work provides a comprehensive map of L-CK1.2 interactions and suggests its potential importance in regulating intracellular <i>Leishmania</i> survival, providing potential targets for leishmaniasis therapy. Furthermore, given the evolutionary conservation of CK1.2 across other parasitic organisms, our findings may have broader implications for understanding and managing parasitic infections.</p></div> 2026-10-05T17:53:02Z Dataset Dataset 10.1371/journal.pone.0356818.t001 https://figshare.com/articles/dataset/pone_0356818_t001_-_p_p_/34073853 CC BY 4.0