Niaz Banaiee1, William R Jacobs, Joel D Ernst. 1. Department of Medicine (Division of Infectious Diseases), NYU School of Medicine, New York, NY 10016, USA. nbanaiee@stanford.edu
Abstract
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>or=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 (DeltalspA::lspAmut) lacking the putative drug target. CONCLUSIONS: Globomycin kills M. tuberculosis through a mechanism that is independent of LspA.
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>or=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 (DeltalspA::lspAmut) lacking the putative drug target. CONCLUSIONS:Globomycin kills M. tuberculosis through a mechanism that is independent of LspA.
Authors: Kelly L Johnston; Bo Wu; Ana Guimarães; Louise Ford; Barton E Slatko; Mark J Taylor Journal: Parasit Vectors Date: 2010-10-14 Impact factor: 3.876