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Nisin depletes ATP and proton motive force in mycobacteria
Author(s) -
Chung H.J.,
Montville T.J.,
Chikindas M.L.
Publication year - 2000
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.2000.00840.x
Subject(s) - nisin , mycobacterium smegmatis , microbiology and biotechnology , mycobacterium bovis , mycobacterium , strain (injury) , biology , efflux , chemiosmosis , intracellular , bacteria , chemistry , biochemistry , antimicrobial , mycobacterium tuberculosis , enzyme , tuberculosis , atp synthase , medicine , genetics , pathology , anatomy
This study examined the inhibitory effect of nisin and its mode of action against Mycobacterium smegmatis , a non‐pathogenic species of mycobacteria, and M. bovis ‐Bacill Carmette Guerin (BCG), a vaccine strain of pathogenic M. bovis . In agar diffusion assays, 2·5 mg ml −1 nisin was required to inhibit M. bovis ‐BCG. Nisin caused a slow, gradual, time‐ and concentration‐dependent decrease in internal ATP levels in M. bovis ‐BCG, but no ATP efflux was detected. In mycobacteria, nisin decreased both components of proton motive force (membrane potential, ΔΨ and ΔpH) in a time‐ and concentration‐dependent manner. However, mycobacteria maintained their intracellular ATP levels during the initial time period of ΔΨ and ΔpH dissipation. These data suggest that the mechanism of nisin in mycobacteria is similar to that in food‐borne pathogens.