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

M C Bopape | Zendy; Helen C. Steel | Zendy; Riana Cockeran | Zendy; N. M. Matlola | Zendy; P. Bernard Fourie | Zendy; Ronald Anderson | Zendy

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

Author(s) -

M C Bopape,

Helen C. Steel,

Riana Cockeran,

N. M. Matlola,

P. Bernard Fourie,

Ronald Anderson

Publication year - 2004

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkh215

Subject(s) - clofazimine , mycobacterium smegmatis , microbiology and biotechnology , mutant , antimicrobial , mycobacterium tuberculosis , chemistry , wild type , mycobacterium , biology , bacteria , biochemistry , tuberculosis , gene , medicine , immunology , leprosy , genetics , pathology

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.

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