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Title2-oxoglutarate:acceptor oxidoreductase-catalyzed redox cycling effectively targets coccoid forms of Helicobacter pylori.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 6965, Year 2025
Publish dateJul 29, 2025
AuthorsXudong Hang / Weiqi Lan / Huang Yanqiang / Hongming Huang / Mingjing Zhang / Liping Zeng / Ting Shi / Yuefan Bai / Zhiyu Yang / Shanwei Hu / Junfan Wang / Linlin Dong / Qian Tong / Jia Jia / Shuzhuang Bi / Qianfeng Xia / Yan Gao / Hongkai Bi /
PubMed AbstractHelicobacter pylori, a globally significant pathogen, plays a central etiological role in diverse gastric pathologies ranging from chronic gastritis and peptic ulcers to gastric adenocarcinoma. ...Helicobacter pylori, a globally significant pathogen, plays a central etiological role in diverse gastric pathologies ranging from chronic gastritis and peptic ulcers to gastric adenocarcinoma. Although conventional antibiotics effectively inhibit or kill growing helical H. pylori, metabolically dormant coccoid forms of H. pylori exhibit considerable tolerance, posing a persistent and clinically significant challenge. Here, we report napabucasin (2-acetylfuro-1,4-naphthoquinone) as a redox-cycling antibiotic with potent bactericidal activity against both drug-resistant helical and coccoid forms of H. pylori. Notably, napabucasin does not induce acquired resistance in vitro and demonstrates superior efficacy compared to standard triple therapy in murine infection models. Mechanistic studies reveal that napabucasin acts through 2-oxoglutarate:acceptor oxidoreductase (OOR)-catalyzed futile redox cycling, generating bactericidal levels of reactive oxygen species (ROS). Compared to menaquinone 6, a proposed physiological electron acceptor, napabucasin exhibits enhanced oxidative capacity. Structural, biochemical, and microbiological analyses identify Leu44 and Lys46 within the OorD subunit as critical residues for napabucasin recognition and catalysis. These findings establish OOR-mediated redox cycling as a robust antimicrobial strategy that sustains endogenous ROS production to combat refractory H. pylori infections.
External linksNat Commun / PubMed:40730563 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.03 Å
Structure data

39556

8ys5

EMDB-39556, PDB-8ys5:
Cryo-EM structure of the Helicobacter pylori OorDABC complex in the apo-form
Method: EM (single particle) / Resolution: 2.95 Å

39557

8ys6

EMDB-39557, PDB-8ys6:
Helicobacter pylori OorDABC in complex with Napabucasin
Method: EM (single particle) / Resolution: 3.03 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MG:
Unknown entry

ChemComp-TPP:
THIAMINE DIPHOSPHATE

PDB-1d65:
MOLECULAR STRUCTURE OF THE B-DNA DODECAMER D(CGCAAATTTGCG)2; AN EXAMINATION OF PROPELLER TWIST AND MINOR-GROOVE WATER STRUCTURE AT 2.2 ANGSTROMS RESOLUTION

Source
  • helicobacter pylori (bacteria)
KeywordsOXIDOREDUCTASE / Oxoglutarate Oxidoreductase / Electron Transport / Tricarboxylic Acid Cycle / Napabucasin

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