Título:
Functional studies of the human protein SQOR, identified as an interactor of the virulence factor PtpA of Mycobacterium tuberculosis
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Autor:
Hergatacorzian, Valentina
Betancour Curutchet, Gabriela
Margenat, Mariana
Cuevasanta, Ernesto
Villarino, Andrea
Betancour Curutchet, Gabriela
Margenat, Mariana
Cuevasanta, Ernesto
Villarino, Andrea
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Tipo de documento:
Póster
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MYCOBACTERIUM TUBERCULOSIS
FOSFATASA
GENES
FOSFATASA
GENES
Año de publicación:
2025
Contenido:
Resumen:
Mycobacterium tuberculosis (Mtb) is the etiological agent of tuberculosis (TB), a disease that has caused the death of 30 million people worldwide in the last 20 years. Mtb can evade the immune response by surviving and replicating within macrophages, introducing various virulence factors into the cytosol. One of these is the tyrosine phosphatase PtpA, which is targeted to the macrophage cytosol during infection and is capable of modulating the innate immune response. Previous reports have shown that PtpA is able to interact with several proteins related to cell metabolism, such as sulfide quinone reductase (hSQOR). This cytosol-produced protein catalyzes H2S oxidation in the mitochondria and is not detected in the organelle during virulent Mtb infection.
Descripción:
Editorial:
Centro de Investigaciones Biomédicas
EN:
International symposium Mitochondria and cell metabolism, Montevideo, 11-12 de junio de 2025.
Financiadores:
FCE_1_2021_1_166706
Citación:
Hergatacorzian, V, Betancour Curutchet, G, Margenat, M, [y otros autores]. Functional studies of the human protein SQOR, identified as an interactor of the virulence factor PtpA of Mycobacterium tuberculosis [en línea] EN: International symposium Mitochondria and cell metabolism, 11-12 de junio de 2025. Montevideo : Centro de Investigaciones Biomédicas, 2025. 1 h
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https://hdl.handle.net/20.500.12008/50746
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Licencia Creative Commons Atribución - No Comercial - Sin Derivadas (CC - By-NC-ND 4.0)
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| Ficheros | Descripción | Tamaño | Formato | ||
|---|---|---|---|---|---|
| Poster Simposio mitocondria 2025.pdf | — | 1.98 MB | Adobe PDF |