<i>Mycobacterium tuberculosis</i> sulfurtransferase <scp>SseA</scp> is activated by its neighboring gene product Rv3284

Tuberculosis remains a critical global health challenge, which underscores the need for new therapeutic targets. A potential drug target is the rhodanese-like thiosulfate sulfurtransferase SseA, which plays a role in macrophage infection by Mycobacterium tuberculosis (Mtb) and its resistance to oxidative stress. In our research, we identified a protein (Rv3284), herein referred to as SufE<sub>Mtb</sub>, that interacts with SseA and modulates its activity. Sequence analysis and molecular modeling revealed that SufE<sub>Mtb</sub> enhances SseA enzymatic function by binding to its non-catalytic N-terminal domain and favoring an activating conformational change in a regulatory loop of SseA. This interaction appears crucial for effective enzyme activity and the maintenance of redox homeostasis in Mtb, making the SseA-SufE<sub>Mtb</sub> complex a potential target for new therapies.

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Publication Details

Journal
FEBS Letters
Published
2025-07-16
DOI
https://doi.org/10.1002/1873-3468.70117
Primary Topic
Pneumocystis jirovecii pneumonia detection and treatment
Type
article
Field-Weighted Citation Impact
0.00

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article

Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284

Giulia Di Napoli, Milagros Medina, Simonetta Oliaro‐Bosso, Salvatore Adinolfi et al.
FEBS Letters
Pneumocystis jirovecii pneumonia detection and treatment
article

Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284

Giulia Di Napoli, Milagros Medina, Simonetta Oliaro‐Bosso, Salvatore Adinolfi, Mauro Marengo, Edoardo Salladini, Alex Fissore, Alessia Ruggiero, Rita Berisio, Adrián Velázquez‐Campoy, Eleonora Raccuia
article en

Abstract

Tuberculosis remains a critical global health challenge, which underscores the need for new therapeutic targets. A potential drug target is the rhodanese-like thiosulfate sulfurtransferase SseA, which plays a role in macrophage infection by Mycobacterium tuberculosis (Mtb) and its resistance to oxidative stress. In our research, we identified a protein (Rv3284), herein referred to as SufE<sub>Mtb</sub>, that interacts with SseA and modulates its activity. Sequence analysis and molecular modeling revealed that SufE<sub>Mtb</sub> enhances SseA enzymatic function by binding to its non-catalytic N-terminal domain and favoring an activating conformational change in a regulatory loop of SseA. This interaction appears crucial for effective enzyme activity and the maintenance of redox homeostasis in Mtb, making the SseA-SufE<sub>Mtb</sub> complex a potential target for new therapies.

FEBS LettersVol. 599(16)
Universidad de Zaragoza (ES), Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (ES), Instituto de Investigación Sanitaria Aragón (ES), Institute of Biostructure and Bioimaging (IT), University of Turin (IT)
European Commission, Università degli Studi di Torino, Ministerio de Medio Ambiente y Medio Rural y Marino, Agencia Estatal de Investigación
Good health and well-being
Openalex Percentile: Top 75%
Pneumocystis jirovecii pneumonia detection and treatment
DOIOpen Access PDFOpenAlex
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