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Narrow-Spectrum Antibiotic Targeting of the Radical SAM Enzyme MqnE in Menaquinone Biosynthesis.
Carl, Ayala G; Harris, Lawrence D; Feng, Mu; Nordstrøm, Lars U; Gerfen, Gary J; Evans, Gary B; Silakov, Alexey; Almo, Steven C; Grove, Tyler L.
Afiliación
  • Carl AG; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
  • Harris LD; The Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand.
  • Feng M; The Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland 5040, New Zealand.
  • Nordstrøm LU; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
  • Gerfen GJ; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
  • Evans GB; Department of Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
  • Silakov A; The Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand.
  • Almo SC; The Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland 5040, New Zealand.
  • Grove TL; Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Biochemistry ; 59(27): 2562-2575, 2020 07 14.
Article en En | MEDLINE | ID: mdl-32627538
Antibiotic resistance continues to spread at an alarming rate, outpacing the introduction of new therapeutics and threatening to globally undermine health care. There is a crucial need for new strategies that selectively target specific pathogens while leaving the majority of the microbiome untouched, thus averting the debilitating and sometimes fatal occurrences of opportunistic infections. To address these challenges, we have adopted a unique strategy that focuses on oxygen-sensitive proteins, an untapped set of therapeutic targets. MqnE is a member of the radical S-adenosyl-l-methionine (RS) superfamily, all of which rely on an oxygen-sensitive [4Fe-4S] cluster for catalytic activity. MqnE catalyzes the conversion of didehydrochorismate to aminofutalosine in the essential menaquinone biosynthetic pathway present in a limited set of species, including the gut pathogen Helicobacter pylori (Hp), making it an attractive target for narrow-spectrum antibiotic development. Indeed, we show that MqnE is inhibited by the mechanism-derived 2-fluoro analogue of didehydrochorismate (2F-DHC) due to accumulation of a radical intermediate under turnover conditions. Structures of MqnE in the apo and product-bound states afford insight into its catalytic mechanism, and electron paramagnetic resonance approaches provide direct spectroscopic evidence consistent with the predicted structure of the radical intermediate. In addition, we demonstrate the essentiality of the menaquinone biosynthetic pathway and unambiguously validate 2F-DHC as a selective inhibitor of Hp growth that exclusively targets MqnE. These data provide the foundation for designing effective Hp therapies and demonstrate proof of principle that radical SAM proteins can be effectively leveraged as therapeutic targets.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: S-Adenosilmetionina / Proteínas Bacterianas / Helicobacter pylori / Vitamina K 2 / Vías Biosintéticas / Radicales Libres / Antibacterianos Idioma: En Revista: Biochemistry Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: S-Adenosilmetionina / Proteínas Bacterianas / Helicobacter pylori / Vitamina K 2 / Vías Biosintéticas / Radicales Libres / Antibacterianos Idioma: En Revista: Biochemistry Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos