2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain

被引:0
作者
Albert Byungyun Jeon
David F. Ackart
Wei Li
Mary Jackson
Roberta J. Melander
Christian Melander
Robert B. Abramovitch
Adam J. Chicco
Randall J. Basaraba
Andrés Obregón-Henao
机构
[1] Immunology,Mycobacteria Research Laboratories, Department of Microbiology
[2] and Pathology,Department of Chemistry
[3] Colorado State University,Department of Microbiology and Molecular Genetics
[4] Fort Collins,Department of Biomedical Sciences
[5] North Carolina State University,College of Veterinary Medicine
[6] Michigan State University,Department of Chemistry & Biochemistry
[7] Colorado State University,undefined
[8] Fort Collins,undefined
[9] University of Florida,undefined
[10] University of Notre Dame,undefined
来源
Scientific Reports | / 9卷
关键词
D O I
暂无
中图分类号
学科分类号
摘要
There is an urgent need to develop new drugs against tuberculosis. In particular, it is critical to target drug tolerant Mycobacterium tuberculosis (M. tuberculosis), responsible, in part, for the lengthy antibiotic regimen required for treatment. We previously postulated that the presence of in vivo biofilm-like communities of M. tuberculosis could contribute to this drug tolerance. Consistent with this hypothesis, certain 2-aminoimidazole (2-AIs) molecules with anti-biofilm activity were shown to revert mycobacterial drug tolerance in an in vitro M. tuberculosis biofilm model. While exploring their mechanism of action, it was serendipitously observed that these 2-AI molecules also potentiated β-lactam antibiotics by affecting mycobacterial protein secretion and lipid export. As these two bacterial processes are energy-dependent, herein it was evaluated if 2-AI compounds affect mycobacterial bioenergetics. At low concentrations, 2B8, the lead 2-AI compound, collapsed both components of the proton motive force, similar to other cationic amphiphiles. Interestingly, however, the minimum inhibitory concentration of 2B8 against M. tuberculosis correlated with a higher drug concentration determined to interfere with the mycobacterial electron transport chain. Collectively, this study elucidates the mechanism of action of 2-AIs against M. tuberculosis, providing a tool to better understand mycobacterial bioenergetics and develop compounds with improved anti-mycobacterial activity.
引用
收藏
相关论文
共 117 条
[1]  
Chopra I(2002)Exploiting current understanding of antibiotic action for discovery of new drugs Journal of applied microbiology 92 Suppl, 4S-15S
[2]  
Hesse L(1998)The outer parts of the mycobacterial envelope as permeability barriers Frontiers in bioscience: a journal and virtual library 3 D1253-1261
[3]  
O’Neill AJ(1991)Permeability of the mycobacterial cell wall Research in microbiology 142 437-443
[4]  
Draper P(1995)The envelope of mycobacteria Annual review of biochemistry 64 29-63
[5]  
Nikaido H(2003)Tuberculosis: a problem with persistence Nature reviews. Microbiology 1 97-105
[6]  
Jarlier V(2013)Dynamic persistence of antibiotic-stressed mycobacteria Science 339 91-95
[7]  
Brennan PJ(2007)Location of persisting mycobacteria in a Guinea pig model of tuberculosis revealed by r207910 Antimicrobial agents and chemotherapy 51 3338-3345
[8]  
Nikaido H(2011)Targeting bacterial membrane function: an underexploited mechanism for treating persistent infections Nature reviews. Microbiology 9 62-75
[9]  
Stewart GR(1957)A new series of phenazines (rimino-compounds) with high antituberculosis activity Nature 179 1013-1015
[10]  
Robertson BD(2005)A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis Science 307 223-227