Examinando por Autor "Ortega, Constanza"

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    Role and Regulation of Clp Proteases: A Target against Gram-Positive Bacteria
    (Multidisciplinary Digital Publishing Institute (MDPI), 2023-03) Queraltó, Camila; Álvarez, Ricardo; Ortega, Constanza; Díaz-Yáñez, Fernando; Paredes-Sabja, Daniel; Gil, Fernando
    Bacterial proteases participate in the proteolytic elimination of misfolded or aggregated proteins, carried out by members of the AAA+ protein superfamily such as Hsp100/Clp, Lon, and FtsH. It is estimated that the Clp and Lon families perform around 80% of cellular proteolysis in bacteria. These functions are regulated, in part, through the spatial and/or temporal use of adapter proteins, which participate in the recognition and delivery of specific substrate proteins to proteases. The proteolysis plays an important role in maintaining and controlling the quality of the proteins, avoiding the accumulation and aggregation of unfolded or truncated proteins. However, this is not their only function, since they play an important role in the formation of virulent phenotypes and in the response to different types of stress faced when entering the host or that occur in the environment. This review summarizes the structural and functional aspects of the Clp proteases and their role in Gram-positive microorganisms. © 2023 by the authors.
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    The chaperone ClpC participates in sporulation, motility, biofilm, and toxin production of Clostridioides difficile
    (Elsevier Ltd, 2023-06) Queraltó, Camila; Ortega, Constanza; Díaz-Yáñez, Fernando; Inostroza, Osvaldo; Espinoza, Giovanni; Álvarez, Ricardo; González, Ruth; Parra, Francisco; Paredes-Sabja, Daniel; Acuña, Lillian G.; Calderón, Iván L.; Fuentes, Juan A.; Gil, Fernando
    Objectives: Clostridioides difficile is a nosocomial pathogen that is associated with the use of antibiotics. One of the most worrying aspects of C. difficile infection is its ability to resist antimicrobial therapies, owing to spore formation. In several bacterial pathogens, proteases of the Clp family participate in phe notypes associated with persistence and virulence. This suggests that these proteins could be involved in virulence-related traits. In this study, we analysed the role of ClpC chaperone-protease of C. difficile in virulence-related traits by comparing the phenotypes of wild-type and mutant strains lacking the clpC gene ( clpC). Methods: We performed biofilm, motility, spore formation, and cytotoxicity assays. Results: Our results show significant differences between the wild-type and clpC strains in all analysed parameters. Conclusions: Based on these findings, we conclude that clpC plays a role in the virulence properties of C. difficile. © 2023 The Author(s). Published by Elsevier Ltd on behalf of International Society for Antimicrobial Chemotherapy. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)