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• W978852152 startingPage "e0133129" @default.
• W978852152 abstract "Mycobacterium tuberculosis is able to utilize cholesterol as a carbon source, and this ability is linked to its virulence in macrophages and in the mouse model of infection. The M. tuberculosis cytochrome P450 Cyp125 plays a key role in cholesterol metabolism being involved in the first steps of its degradation. Cyp125 is a cholesterol hydroxylase which is essential for cholesterol catabolism in M. bovis BCG and some strains of M. tuberculosis. We generated an unmarked, in-frame deletion of Cyp125 in M. tuberculosis H37Rv. The deletion strain was able to grow as well as wild-type in medium containing glucose as the carbon source. The Cyp125 deletion strain was more sensitive to growth inhibition by clotrimazole consistent with the ability of Cyp125 to bind azoles with high affinity. The deletion strain showed no difference in sensitivity to nitric oxide or hydrogen peroxide and was not attenuated for growth inside THP-1 human macrophage-like cells. These data suggest that the attenuation of virulence seen in operon deletion strains is not linked to the lack of Cyp125 alone." @default.
• W978852152 created "2016-06-24" @default.
• W978852152 creator A5036429812 @default.
• W978852152 creator A5056475928 @default.
• W978852152 date "2015-07-21" @default.
• W978852152 modified "2023-10-17" @default.
• W978852152 title "Deletion of cyp125 Confers Increased Sensitivity to Azoles in Mycobacterium tuberculosis" @default.
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• W978852152 doi "https://doi.org/10.1371/journal.pone.0133129" @default.
• W978852152 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4510303" @default.
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