Journal Article

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 and R. Anderson

in Journal of Antimicrobial Chemotherapy

Published on behalf of British Society for Antimicrobial Chemotherapy

Volume 53, issue 6, pages 971-974
Published in print June 2004 | ISSN: 0305-7453
Published online June 2004 | e-ISSN: 1460-2091 | DOI: http://dx.doi.org/10.1093/jac/dkh215
Antimicrobial activity of clofazimine is not dependent on mycobacterial C-type phospholipases

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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.

Keywords: Keywords: mycobacteria, phospholipase C, Mycobacterium tuberculosis, Mycobacterium smegmatis

Journal Article.  2422 words.  Illustrated.

Subjects: Medical Oncology ; Critical Care

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