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Antimicrobial activity of clofazimine is not dependent on mycobacterial C-type phospholipases.
- Source :
-
The Journal of antimicrobial chemotherapy [J Antimicrob Chemother] 2004 Jun; Vol. 53 (6), pp. 971-4. Date of Electronic Publication: 2004 Apr 29. - Publication Year :
- 2004
-
Abstract
- We have used a phospholipase C (PLC)-deletion mutant (plcABC) of the H37Rv strain of Mycobacterium tuberculosis (MTB), as well as a plcA-insertion mutant of Mycobacterium smegmatis, to investigate the possible involvement of PLCs in clofazimine-mediated inhibition of mycobacterial K(+) transport and growth. Inactivation of the PLCs of MTB and insertion of the plcA gene into M. smegmatis resulted in a substantial reduction and increase in hydrolysis of phosphatidylcholine (PC), respectively. However, both the mutant and wild-type strains of MTB and M. smegmatis were equally sensitive to the inhibitory effects of clofazimine on K(+) uptake and growth. These observations demonstrate that the PLCs of MTB are not involved in the antimicrobial activity of clofazimine.
- Subjects :
- Arachidonic Acid metabolism
Cyclohexanones pharmacology
Gene Deletion
Hydrolysis
Lipoprotein Lipase antagonists & inhibitors
Mycobacterium smegmatis drug effects
Mycobacterium smegmatis enzymology
Mycobacterium smegmatis genetics
Mycobacterium tuberculosis genetics
Rubidium Radioisotopes
Type C Phospholipases genetics
Anti-Infective Agents pharmacology
Clofazimine pharmacology
Mycobacterium tuberculosis drug effects
Mycobacterium tuberculosis enzymology
Type C Phospholipases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0305-7453
- Volume :
- 53
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- The Journal of antimicrobial chemotherapy
- Publication Type :
- Academic Journal
- Accession number :
- 15117926
- Full Text :
- https://doi.org/10.1093/jac/dkh215