Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis.

نویسندگان

  • Vadim Makarov
  • Giulia Manina
  • Katarina Mikusova
  • Ute Möllmann
  • Olga Ryabova
  • Brigitte Saint-Joanis
  • Neeraj Dhar
  • Maria Rosalia Pasca
  • Silvia Buroni
  • Anna Paola Lucarelli
  • Anna Milano
  • Edda De Rossi
  • Martina Belanova
  • Adela Bobovska
  • Petronela Dianiskova
  • Jana Kordulakova
  • Claudia Sala
  • Elizabeth Fullam
  • Patricia Schneider
  • John D McKinney
  • Priscille Brodin
  • Thierry Christophe
  • Simon Waddell
  • Philip Butcher
  • Jakob Albrethsen
  • Ida Rosenkrands
  • Roland Brosch
  • Vrinda Nandi
  • Sowmya Bharath
  • Sheshagiri Gaonkar
  • Radha K Shandil
  • Venkataraman Balasubramanian
  • Tanjore Balganesh
  • Sandeep Tyagi
  • Jacques Grosset
  • Giovanna Riccardi
  • Stewart T Cole
چکیده

New drugs are required to counter the tuberculosis (TB) pandemic. Here, we describe the synthesis and characterization of 1,3-benzothiazin-4-ones (BTZs), a new class of antimycobacterial agents that kill Mycobacterium tuberculosis in vitro, ex vivo, and in mouse models of TB. Using genetics and biochemistry, we identified the enzyme decaprenylphosphoryl-beta-d-ribose 2'-epimerase as a major BTZ target. Inhibition of this enzymatic activity abolishes the formation of decaprenylphosphoryl arabinose, a key precursor that is required for the synthesis of the cell-wall arabinans, thus provoking cell lysis and bacterial death. The most advanced compound, BTZ043, is a candidate for inclusion in combination therapies for both drug-sensitive and extensively drug-resistant TB.

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Development of a quantitative assay for mycobacterial endogenous arabinase and ensuing studies of arabinase levels and arabinan metabolism in Mycobacterium smegmatis.

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The benzothiazinone lead compound, BTZ043, kills Mycobacterium tuberculosis by inhibiting the essential flavo-enzyme DprE1, decaprenylphosphoryl-beta-D-ribose 2-epimerase. Here, we synthesized a new series of piperazine-containing benzothiazinones (PBTZ) and show that, like BTZ043, the preclinical candidate PBTZ169 binds covalently to DprE1. The crystal structure of the DprE1-PBTZ169 complex re...

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عنوان ژورنال:
  • Science

دوره 324 5928  شماره 

صفحات  -

تاریخ انتشار 2009