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JAC Advance Access originally published online on June 19, 2007
Journal of Antimicrobial Chemotherapy 2007 60(2):414-416; doi:10.1093/jac/dkm223
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© The Author 2007. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

LspA-independent action of globomycin on Mycobacterium tuberculosis

Niaz Banaiee1,*, William R. Jacobs2 and Joel D. Ernst1,3

1 Department of Medicine (Division of Infectious Diseases), NYU School of Medicine, New York, NY 10016, USA 2 Howard Hughes Medical Institute and Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA 3 Department of Microbiology, NYU School of Medicine, New York, NY 10016, USA

Received 25 March 2007; returned 2 May 2007; revised 16 May 2007; accepted 25 May 2007

* Correspondence address. Department of Pathology, Stanford University School of Medicine, 3375 Hillview Avenue, Room 1602, Palo Alto, CA 94304, USA. Tel: +1-650-736-8052; Fax: +1-650-725-5671; E-mail: nbanaiee{at}stanford.edu

Objectives: The objective of this study was to investigate the antimicrobial activity and specificity of globomycin, an inhibitor of lipoprotein signal peptidase II (LspA), against Mycobacterium tuberculosis.

Methods: The mycobactericidal and mycobacteriostatic activity of globomycin was determined by optical density and cfu plating. The specificity of globomycin was determined by western immunoblotting using anti-MPT83 antibody.

Results: Globomycin is mycobactericidal at concentrations ≥40 mg/L. However, at 80 mg/L, the processing of the lipoprotein MPT-83 is unaffected and growth-inhibitory effect of globomycin is unchanged in an lspA null mutant ({Delta}lspA::lspAmut) lacking the putative drug target.

Conclusions: Globomycin kills M. tuberculosis through a mechanism that is independent of LspA.

Keywords: lipoproteins , lipoprotein signal peptidase , lipoprotein processing , antimycobacterials


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