Skip Navigation


JAC Advance Access originally published online on April 29, 2004
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
53/6/971    most recent
dkh215v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (3)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Bopape, M. C.
Right arrow Articles by Anderson, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bopape, M. C.
Right arrow Articles by Anderson, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?


Journal of Antimicrobial Chemotherapy (2004) 53, 971-974
© 2004 The British Society for Antimicrobial Chemotherapy

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

M. C. Bopape1, H. C. Steel2, R. Cockeran2, N. M. Matlola2, P. B. Fourie1 and R. Anderson2,*

1 Tuberculosis Research Lead Programme, Medical Research Council, Pretoria; 2 Medical Research Council Unit for Inflammation and Immunity, Department of Immunology, Faculty of Health Sciences, University of Pretoria, PO Box 2034, Pretoria 0001, South Africa

Received 21 November 2003; accepted 27 February 2004

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: mycobacteria, phospholipase C, Mycobacterium tuberculosis, Mycobacterium smegmatis

* Corresponding author. Tel: +27-12-319-2425; Fax: +27-12-323-0732; E-mail: randerso{at}medic.up.ac.za


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
S. K. Parker, K. M. Curtin, and M. L. Vasil
Purification and Characterization of Mycobacterial Phospholipase A: an Activity Associated with Mycobacterial Cutinase
J. Bacteriol., June 1, 2007; 189(11): 4153 - 4160.
[Abstract] [Full Text] [PDF]

Home page
 J Antimicrob ChemotherHome page
M. C. Cholo, H. I. Boshoff, H. C. Steel, R. Cockeran, N. M. Matlola, K. J. Downing, V. Mizrahi, and R. Anderson
Effects of clofazimine on potassium uptake by a Trk-deletion mutant of Mycobacterium tuberculosis
J. Antimicrob. Chemother., January 1, 2006; 57(1): 79 - 84.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.