Título:
Interaction between PtpA and SQOR: a potential mycobacterial strategy to modulate host sulfide metabolism
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Autor:
Hergatacorzian, Valentina
Herrera, Fernando E.
Bentancour, Gabriela
Margenat, Mariana
Boschi-Muller, Sandrine
Selles, Benjamin
Cuevasanta, Ernesto
Villarino, Andrea
Herrera, Fernando E.
Bentancour, Gabriela
Margenat, Mariana
Boschi-Muller, Sandrine
Selles, Benjamin
Cuevasanta, Ernesto
Villarino, Andrea
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Tipo de documento:
Póster
Editor:
Palabras clave:
Fosfatasa
Mycobacterium Tuberculosis
SQOR
Mitocondria
Mycobacterium Tuberculosis
SQOR
Mitocondria
Descriptores:
Año de publicación:
2026
Contenido:
Resumen:
Hydrogen sulfide (H2S) is involved in numerous pathophysiological processes; however, the role of host-derived H2S in microbial pathogenesis remains poorly understood. It has been reported that during infection with a virulent strain of Mycobacterium tuberculosis (Mtb), the protein sulfide:quinone oxidoreductase (SQOR), a key enzyme in eukaryotic H2S consumption, is no longer detected in the mitochondria. Moreover, our group previously identified SQOR as an interactor of the tyrosine phosphatase PtpA, a well-known virulence factor of Mtb capable of reaching the cytosol of macrophages during infection. This could suggest that PtpA, by dephosphorylating some tyrosine of hSQOR, causes a change in the subcellular localization and/or activity of this eukaryotic protein. A potential inhibition of SQOR by PtpA could elevate H2S levels in eukaryotic cells, a condition previously reported to enhance bacterial survival and success during infection. To elucidate how PtpA modulates SQOR activity, we first modeled the interaction in silico. By measuring electrostatic interacting energy using the Adaptive Poisson-Boltzmann Solver (APBS) we identified a specific phosphotyrosine (p-Tyr 434) residue within SQOR as the potential PtpA target. Subsequently, we produced several recombinant SQOR (rSQOR) variants to evaluate their phosphorylation states and enzymatic activity following treatment with the mycobacterial phosphatase. Furthermore, we generated the plasmids necessary to validate the SQOR-PtpA interaction in a cellular context using Bimolecular Fluorescence Complementation (BiFC) assays. Our work aims to contribute to understanding the mycobacterium-host molecular interactions to identify treatment targets in infections.
Descripción:
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Instituto Pasteur
EN:
EMBO Workshop, Francia 14-18 septiembre 2026.
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ANII: POS_NAC_2024_1_183729.
Citación:
Hergatacorzian, V., Herrera, F., Bentancour, G. [y otros autores]. Interaction between PtpA and SQOR: a potential mycobacterial strategy to modulate host sulfide metabolism [en línea] EN: EMBO Workshop, Francia 14-18 septiembre 2026. Instituto Pasteur - París, 2026 . 1 h .
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Attribution-NonCommercial-NoDerivatives 4.0 International
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| Ficheros | Descripción | Tamaño | Formato | ||
|---|---|---|---|---|---|
| Principal Poster EMBO.pdf | — | 2.35 MB | Adobe PDF |
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