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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

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.[1]

References

  1. Antimicrobial activity of clofazimine is not dependent on mycobacterial C-type phospholipases. Bopape, M.C., Steel, H.C., Cockeran, R., Matlola, N.M., Fourie, P.B., Anderson, R. J. Antimicrob. Chemother. (2004) [Pubmed]
 
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