Relevant bibliographies by topics / M. smegmatis - Rifampicin

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Academic literature on the topic 'M. smegmatis - Rifampicin'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "M. smegmatis - Rifampicin"

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Do, Thi Thuy, Jerónimo Rodríguez-Beltran, Esmeralda Cebrián-Sastre, Alexandro Rodríguez-Rojas, Alfredo Castañeda-García, and Jesús Blázquez. "Inactivation of a New Potassium Channel Increases Rifampicin Resistance and Induces Collateral Sensitivity to Hydrophilic Antibiotics in Mycobacterium smegmatis." Antibiotics 11, no. 4 (2022): 509. http://dx.doi.org/10.3390/antibiotics11040509.

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Rifampicin is a critical first-line antibiotic for treating mycobacterial infections such as tuberculosis, one of the most serious infectious diseases worldwide. Rifampicin resistance in mycobacteria is mainly caused by mutations in the rpoB gene; however, some rifampicin-resistant strains showed no rpoB mutations. Therefore, alternative mechanisms must explain this resistance in mycobacteria. In this work, a library of 11,000 Mycobacterium smegmatis mc2 155 insertion mutants was explored to search and characterize new rifampicin-resistance determinants. A transposon insertion in the MSMEG_194
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Dey, Abhinav, Amit Kumar Verma, and Dipankar Chatterji. "Role of an RNA polymerase interacting protein, MsRbpA, from Mycobacterium smegmatis in phenotypic tolerance to rifampicin." Microbiology 156, no. 3 (2010): 873–83. http://dx.doi.org/10.1099/mic.0.033670-0.

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Rifampicin and its derivatives are at the forefront of the current standard chemotherapeutic regimen for active tuberculosis; they act by inhibiting the transcription activity of prokaryotic RNA polymerase. Rifampicin is believed to interact with the β subunit of RNA polymerase. However, it has been observed that protein–protein interactions with RNA polymerase core enzyme lead to its reduced susceptibility to rifampicin. This mechanism became more diversified with the discovery of RbpA, a novel RNA polymerase-binding protein, in Streptomyces coelicolor that could mitigate the effect of rifamp
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Kurthkoti, Krishna, Thiruneelakantan Srinath, Pradeep Kumar, et al. "A distinct physiological role of MutY in mutation prevention in mycobacteria." Microbiology 156, no. 1 (2010): 88–93. http://dx.doi.org/10.1099/mic.0.033621-0.

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Oxidative damage to DNA results in the occurrence of 7,8-dihydro-8-oxoguanine (8-oxoG) in the genome. In eubacteria, repair of such damage is initiated by two major base-excision repair enzymes, MutM and MutY. We generated a MutY-deficient strain of Mycobacterium smegmatis to investigate the role of this enzyme in DNA repair. The MutY deficiency in M. smegmatis did not result in either a noteworthy susceptibility to oxidative stress or an increase in the mutation rate. However, rifampicin-resistant isolates of the MutY-deficient strain showed distinct mutations in the rifampicin-resistance-det
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Tran, Huyen Thi, Julia Solnier, Eva-Maria Pferschy-Wenzig, et al. "Antimicrobial and Efflux Pump Inhibitory Activity of Carvotacetones from Sphaeranthus africanus Against Mycobacteria." Antibiotics 9, no. 7 (2020): 390. http://dx.doi.org/10.3390/antibiotics9070390.

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Carvotacetones (1–7) isolated from Sphaeranthus africanus were screened for their antimycobacterial and efflux pump (EP) inhibitory potential against the mycobacterial model strains Mycobacterium smegmatis mc2 155, Mycobacterium aurum ATCC 23366, and Mycobacterium bovis BCG ATCC 35734. The minimum inhibitory concentrations (MICs) of the carvotacetones were detected through high-throughput spot culture growth inhibition (HT-SPOTi) and microbroth dilution assays. In order to assess the potential of the compounds 1 and 6 to accumulate ethidium bromide (EtBr) in M. smegmatis and M. aurum, a microt
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Verma, Amit Kumar, and Dipankar Chatterji. "Dual role of MsRbpA: transcription activation and rescue of transcription from the inhibitory effect of rifampicin." Microbiology 160, no. 9 (2014): 2018–29. http://dx.doi.org/10.1099/mic.0.079186-0.

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MsRbpA is an RNA polymerase (RNAP) binding protein from Mycobacterium smegmatis. According to previous studies, MsRbpA rescues rifampicin-induced transcription inhibition upon binding to the RNAP. Others have shown that RbpA from Mycobacterium tuberculosis (MtbRbpA) is a transcription activator. In this study, we report that both MsRbpA and MtbRbpA activate transcription as well as rescue rifampicin-induced transcription inhibition. Transcription activation is achieved through the increased formation of closed RNAP–promoter complex as well as enhanced rate of conversion of this complex to a st
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6

Nastenko, Volodymyr. "Antimycobacterial activity of new aryloxyethoxy-dialkylaminopropanol derivatives against reference strains of nontuberculous mycobacteria." ScienceRise: Biological Science, no. 1 (42) (April 10, 2025): 12–17. https://doi.org/10.15587/2519-8025.2025.326435.

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Objective. To evaluate the in vitro antimycobacterial activity of novel quaternary ammonium salts, derived from alkyl(aryloxyethoxy)dialkylaminopropanol against reference strains of nontuberculous mycobacteria (NTM). Materials and Methods. A total of 52 synthesized compounds, obtained via phase-transfer catalysis, were studied,. The activity was assessed in two stages: initial screening using the agar diffusion method (well method), followed by minimum inhibitory concentration (MIC) determination through serial dilution. Primary testing was performed on Mycobacterium smegmatis, followed by eva
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Solnier, Julia, Liam Martin, Sanjib Bhakta, and Franz Bucar. "Flavonoids as Novel Efflux Pump Inhibitors and Antimicrobials Against Both Environmental and Pathogenic Intracellular Mycobacterial Species." Molecules 25, no. 3 (2020): 734. http://dx.doi.org/10.3390/molecules25030734.

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Therapeutic treatment options for opportunistic non-tuberculous mycobacterial (NTM) infection and/or serious mycobacterial infections such as tuberculosis (TB) and leprosy are limited due to the spread of antimicrobial resistance mechanism. Plant-derived natural compounds as prospective efflux pump inhibitors may present a promising adjunct to conventional chemotherapy by enhancing mycobacterial susceptibility to antibiotics. This study served to evaluate the antimicrobial and resistance-modifying profile of a range of plant-derived flavonoids against the mycobacterial model strains: M. smegma
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Sachan, Tarun Kumar, and Virendra Kumar. "Antibiotic Susceptibility in Biofilms of Mycobacterium smegmatis." International Journal of Applied Sciences and Biotechnology 3, no. 4 (2015): 635–41. http://dx.doi.org/10.3126/ijasbt.v3i4.13522.

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In the present article we observed the quantification and morphological, ultrastructural features of biofilms of fast growing clinical isolates M. smegmatis in presence of first line antibacterial drug streptomycin, isoniazid rifampicin, ethambutol and pyrazinamide. Biofilm of M. smegmatis was found to be unaffected at concentration of drugs that inhibited growth of planktonic bacilli .Thus, the biofilm growth modus appears to be a strategy for replicating bacilli to evade the trap of antibacterials. Planktonic and biofilm cells had similar intrinsic antibiotic susceptibility. Electron microsc
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Tamuhla, Tsaone, Lydia Joubert, Danicke Willemse, and Monique J. Williams. "SufT is required for growth of Mycobacterium smegmatis under iron limiting conditions." Microbiology 166, no. 3 (2020): 296–305. http://dx.doi.org/10.1099/mic.0.000881.

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Iron-sulphur (FeS) clusters are versatile cofactors required for a range of biological processes within cells. Due to the reactive nature of the constituent molecules, assembly and delivery of these cofactors requires a multi-protein machinery in vivo. In prokaryotes, SufT homologues are proposed to function in the maturation and transfer of FeS clusters to apo-proteins. This study used targeted gene deletion to investigate the role of SufT in the physiology of mycobacteria, using Mycobacterium smegmatis as a model organism. Deletion of the sufT gene in M. smegmatis had no impact on growth und
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10

Kunota, Tafara T. R., Md Aejazur Rahman, Barry E. Truebody, et al. "Mycobacterium tuberculosis H2S Functions as a Sink to Modulate Central Metabolism, Bioenergetics, and Drug Susceptibility." Antioxidants 10, no. 8 (2021): 1285. http://dx.doi.org/10.3390/antiox10081285.

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H2S is a potent gasotransmitter in eukaryotes and bacteria. Host-derived H2S has been shown to profoundly alter M. tuberculosis (Mtb) energy metabolism and growth. However, compelling evidence for endogenous production of H2S and its role in Mtb physiology is lacking. We show that multidrug-resistant and drug-susceptible clinical Mtb strains produce H2S, whereas H2S production in non-pathogenic M. smegmatis is barely detectable. We identified Rv3684 (Cds1) as an H2S-producing enzyme in Mtb and show that cds1 disruption reduces, but does not eliminate, H2S production, suggesting the involvement
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Dissertations / Theses on the topic "M. smegmatis - Rifampicin"

1

Sharmada, S. "Cellular and Molecular Features of the Response of Mycobacterium smegmatis to Rifampicin and Moxifloxacin Upon Prolonged Exposure." Thesis, 2017. http://etd.iisc.ac.in/handle/2005/4168.

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Bacterial persisters are a subpopulation of bacteria that can tolerate lethal concentrations of antibiotics. These are phenotypic variants that can give rise to drug‐susceptible population upon withdrawal of the antibiotic. Persistent bacteria play a crucial role in prolonging antibiotic treatment and are responsible for the recalcitrance of many chronic bacterial diseases, including tuberculosis. Several mechanisms have been proposed for the formation of persisters, which include expression of toxin‐antitoxin systems, generation of reactive oxygen species (ROS), and stochastic changes in gene
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Dey, Abhinav. "Role of an RNA Polymerase Interacting Protein, MsRbpA, from Mycobacterium smegmatis in Phenotypic Tolerance to Rifampicin." Thesis, 2010. https://etd.iisc.ac.in/handle/2005/4621.

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Rifampicin is a non-competitive inhibitor of bacterial RNA polymerase (RNAP). The knowledge about the mechanism of action of this drug has emanated from the genetic and the biochemical studies carried out on Escherichia coli RNAP. The complete picture about the steric mechanism was obtained from structural studies on Thermus aquaticus core RNAP in complex with rifampicin. Resistance to rifampicin has been attributed to mutations in its binding pocket lying within the β-subunit of RNAP. The phenomenon of molecular tolerance to this drug came to light with the discovery of differential inhibitio
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3

Verma, Amit Kumar. "Elucidating the Role of MsRbpA in Rifampicin Tolerance and Transcription Regulation of Mycobacterium Smegmatis." Thesis, 2013. http://etd.iisc.ac.in/handle/2005/3397.

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RNA polymerase binding protein A (RbpA) was first discovered as a RNA polymerase binding protein from Streptomyces. coelicolor. It was shown to cause rifampicin tolerance to RNA polymerase in vitro and leads to basal level of rifampicin resistance in vivo. This protein is exclusively present in the actinobacteria family with the nearest neighbour in mycobacteria. When null mutant of RbpA in S. coelicolor were transformed with the rbpA gene from Mycobacterium tuberculosis the resistance level of rifampicin increased from 0.75 µgml-1 to 2 µg ml-1 suggesting analogous role of MtbRbpA (RbpA from M
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Verma, Amit Kumar. "Elucidating the Role of MsRbpA in Rifampicin Tolerance and Transcription Regulation of Mycobacterium Smegmatis." Thesis, 2013. http://etd.iisc.ernet.in/2005/3397.

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Abstract:
RNA polymerase binding protein A (RbpA) was first discovered as a RNA polymerase binding protein from Streptomyces. coelicolor. It was shown to cause rifampicin tolerance to RNA polymerase in vitro and leads to basal level of rifampicin resistance in vivo. This protein is exclusively present in the actinobacteria family with the nearest neighbour in mycobacteria. When null mutant of RbpA in S. coelicolor were transformed with the rbpA gene from Mycobacterium tuberculosis the resistance level of rifampicin increased from 0.75 µgml-1 to 2 µg ml-1 suggesting analogous role of MtbRbpA (RbpA from M
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