Journal of Antimicrobial Chemotherapy 2004-06-01

Antimicrobial activity of clofazimine is not dependent on mycobacterial C-type phospholipases.

M C Bopape, H C Steel, R Cockeran, N M Matlola, P B Fourie, R Anderson

Index: J. Antimicrob. Chemother. 53(6) , 971-4, (2004)

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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.

Related Compounds

  • RHC-80267

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