Proposed contribution of Rv1819c an efflux pump (ABC protein) from Mycobacterium tuberculosis to drug efflux in Corynebacterium glutamicum

2013 ◽  
Vol 4 (2) ◽  
pp. 28-36
Author(s):  
Sungai Mazando ◽  
M. Zimba ◽  
C. Zimudzi ◽  
S. Dumbura ◽  
M. Gundidza
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Corynebacterium Glutamicum ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Abc Protein

scholarly journals Characterization of P55, a Multidrug Efflux Pump inMycobacterium bovis and Mycobacterium tuberculosis

2001 ◽  
Vol 45 (3) ◽  
pp. 800-804 ◽  
Author(s):  
Pedro E. A. Silva ◽  
Fabiana Bigi ◽  
Marı́a de la Paz Santangelo ◽  
Maria Isabel Romano ◽  
Carlos Martı́n ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Mycobacterium Smegmatis ◽  
Efflux Pump ◽  
Tetracycline Resistance ◽  
Drug Efflux ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Reading Frame ◽  
Carbonyl Cyanide

ABSTRACT The Mycobacterium bovis P55 gene, located downstream from the gene that encodes the immunogenic lipoprotein P27, has been characterized. The gene was identical to the open reading frame of the Rv1410c gene in the genome of Mycobacterium tuberculosisH37Rv, annotated as a probable drug efflux protein. Genes similar toP55 were present in all species of the M. tuberculosis complex and other mycobacteria such asMycobacterium leprae and Mycobacterium avium. By Western blotting, P55 was located in the membrane fraction ofM. bovis. When transformed into Mycobacterium smegmatis after cloning, P55 conferred aminoglycoside and tetracycline resistance. The levels of resistance to streptomycin and tetracycline conferred by P55 were decreased in the presence of the protonophore carbonyl cyanide m-chlorophenylhydrazone and the pump inhibitors verapamil and reserpine. M. smegmatiscells expressing the plasmid-encoded P55 accumulated less tetracycline than the control cells. We conclude that P55 is a membrane protein implicated in aminoglycoside and tetracycline efflux in mycobacteria.

scholarly journals Mutation ofRv2887, amarR-Like Gene, Confers Mycobacterium tuberculosis Resistance to an Imidazopyridine-Based Agent

2015 ◽  
Vol 59 (11) ◽  
pp. 6873-6881 ◽  
Author(s):  
Kathryn Winglee ◽  
Shichun Lun ◽  
Marco Pieroni ◽  
Alan Kozikowski ◽  
William Bishai
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Drug Targets ◽  
Efflux Pump ◽  
Transcriptional Regulator ◽  
Cross Resistance ◽  
Loss Of Function ◽  
Strong Activity ◽  
Content Type ◽  
Novel Drug

ABSTRACTDrug resistance is a major problem inMycobacterium tuberculosiscontrol, and it is critical to identify novel drug targets and new antimycobacterial compounds. We have previously identified an imidazo[1,2-a]pyridine-4-carbonitrile-based agent, MP-III-71, with strong activity againstM. tuberculosis. In this study, we evaluated mechanisms of resistance to MP-III-71. We derived three independentM. tuberculosismutants resistant to MP-III-71 and conducted whole-genome sequencing of these mutants. Loss-of-function mutations inRv2887were common to all three MP-III-71-resistant mutants, and we confirmed the role ofRv2887as a gene required for MP-III-71 susceptibility using complementation. The Rv2887 protein was previously unannotated, but domain and homology analyses suggested it to be a transcriptional regulator in the MarR (multiple antibiotic resistance repressor) family, a group of proteins first identified inEscherichia colito negatively regulate efflux pumps and other mechanisms of multidrug resistance. We found that two efflux pump inhibitors, verapamil and chlorpromazine, potentiate the action of MP-III-71 and that mutation ofRv2887abrogates their activity. We also used transcriptome sequencing (RNA-seq) to identify genes which are differentially expressed in the presence and absence of a functional Rv2887 protein. We found that genes involved in benzoquinone and menaquinone biosynthesis were repressed by functional Rv2887. Thus, inactivating mutations ofRv2887, encoding a putative MarR-like transcriptional regulator, confer resistance to MP-III-71, an effective antimycobacterial compound that shows no cross-resistance to existing antituberculosis drugs. The mechanism of resistance ofM. tuberculosisRv2887mutants may involve efflux pump upregulation and also drug methylation.

Molecular modelling and competitive inhibition of a Mycobacterium tuberculosis multidrug-resistance efflux pump

2019 ◽  
Vol 87 ◽  
pp. 98-108 ◽  
Author(s):  
Joāo Luís Rheingantz Scaini ◽  
Alex Dias Camargo ◽  
Vinicius Rosa Seus ◽  
Andrea von Groll ◽  
Adriano Velasque Werhli ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Multidrug Resistance ◽  
Molecular Modelling ◽  
Efflux Pump ◽  
Competitive Inhibition

scholarly journals Molecular modelling and simulation studies of the Mycobacterium tuberculosis multidrug efflux pump protein Rv1258c

PLoS ONE ◽  
2018 ◽  
Vol 13 (11) ◽  
pp. e0207605 ◽  
Author(s):  
Ruben Cloete ◽  
Erika Kapp ◽  
Jacques Joubert ◽  
Alan Christoffels ◽  
Sarel F. Malan
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Molecular Modelling ◽  
Efflux Pump ◽  
Modelling And Simulation ◽  
Simulation Studies ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump

Evaluation of efflux pump gene expression among drug susceptible and drug resistant strains of Mycobacterium tuberculosis from Iran

2015 ◽  
Vol 36 ◽  
pp. 23-26 ◽  
Author(s):  
Jalil Kardan Yamchi ◽  
Mehri Haeili ◽  
Seifu Gizaw Feyisa ◽  
Hossein Kazemian ◽  
Abdolrazagh Hashemi Shahraki ◽  
...  
Keyword(s):  
Gene Expression ◽  
Mycobacterium Tuberculosis ◽  
Efflux Pump ◽  
Drug Resistant ◽  
Resistant Strains ◽  
Drug Resistant Strains

P-glycoprotein as the drug efflux pump in primary cultured bovine brain capillary endothelial cells

Life Sciences ◽  
1992 ◽  
Vol 51 (18) ◽  
pp. 1427-1437 ◽  
Author(s):  
Akira Tsuji ◽  
Tetsuya Terasaki ◽  
Yasushi Takabatake ◽  
Yoshiyuki Tenda ◽  
Ikumi Tamai ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Efflux Pump ◽  
Bovine Brain ◽  
Drug Efflux ◽  
Brain Capillary ◽  
Brain Capillary Endothelial Cells ◽  
P Glycoprotein ◽  
Capillary Endothelial Cells ◽  
Drug Efflux Pump

Structure-property correlation in gallic acid and 4-cyanopyridine cocrystal and binding studies with drug efflux pump in bacteria

2021 ◽  
Vol 1225 ◽  
pp. 129279
Author(s):  
Shyam Goswami ◽  
Arabinda Ghosh ◽  
Karmajyoti Borah ◽  
Anupam Mahanta ◽  
Ankur K Guha ◽  
...  
Keyword(s):  
Gallic Acid ◽  
Efflux Pump ◽  
Drug Efflux ◽  
Structure Property ◽  
Binding Studies ◽  
Property Correlation ◽  
Drug Efflux Pump
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