| Literature DB >> 28760899 |
Atica Moosa1, Dirk A Lamprecht2, Kriti Arora3, Clifton E Barry3,4, Helena I M Boshoff3, Thomas R Ioerger5, Adrie J C Steyn2,6,7, Valerie Mizrahi1,4, Digby F Warner8,4.
Abstract
We deleted subunits I (cydA) and II (cydB) of the Mycobacterium tuberculosis cytochrome bd menaquinol oxidase. The resulting ΔcydA and ΔcydAB mutants were hypersusceptible to compounds targeting the mycobacterial bc1 menaquinol-cytochrome c oxidoreductase and exhibited bioenergetic profiles indistinguishable from strains deficient in the ABC-type transporter, CydDC, predicted to be essential for cytochrome bd assembly. These results confirm CydAB and CydDC as potential targets for drugs aimed at inhibiting a terminal respiratory oxidase implicated in pathogenesis.Entities:
Keywords: TB drug discovery; electron transport chain; extracellular flux analysis; mycobacterial respiration; oxidative phosphorylation
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Year: 2017 PMID: 28760899 PMCID: PMC5610507 DOI: 10.1128/AAC.01338-17
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191