ArticleAntimicrobial agents and chemotherapy2004
Multidrug resistance of a porin deletion mutant of Mycobacterium smegmatis.
Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 115 citations in OpenAlex.
- Advancements in Technologies Targeting Horizontal Gene TransferRoutes to Control Drug Resistance Evolution.ACS bio & med chem Au · 2026Review
- PE/PPE proteins contribute to Mycobacterium tuberculosis drug resistance.Nature communications · 2026Article
- The accessory role of the outer membrane porin protein MspD inMicrobiology (Reading, England) · 2026Article
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Durlobactam to boost the clinical utility of standard of care β-lactams againstAntimicrobial agents and chemotherapy · 2025Article
- Cephalosporin resistance, tolerance, and approaches to improve their activities.The Journal of antibiotics · 2024Review
- Evolution ofVirulence · 2023Article
- Acyldepsipeptide Analogues: A Future Generation Antibiotics for Tuberculosis Treatment.Pharmaceutics · 2022Review
- Total Synthesis of Tetrahydrolipstatin, Its Derivatives, and Evaluation of Their Ability to Potentiate Multiple Antibiotic Classes againstACS infectious diseases · 2021Article
- Atypically Modified Carbapenem Antibiotics Display Improved Antimycobacterial Activity in the Absence of β-Lactamase Inhibitors.ACS infectious diseases · 2021Article
- Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope.Chemical reviews · 2021Review
- Review
- Phosphorylation on PstP Regulates Cell Wall Metabolism and Antibiotic Tolerance in Mycobacterium smegmatis.Journal of bacteriology · 2021Article
- Increased Virulence of Outer Membrane Porin Mutants ofFrontiers in microbiology · 2021Article
- Identification and Characterization of Mycobacterial Species Using Whole-Genome Sequences.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Mechanisms of Drug-Induced Tolerance in Mycobacterium tuberculosis.Clinical microbiology reviews · 2020Review
- Recovery of Non-tuberculous Mycobacteria from Water is Influenced by Phenotypic Characteristics and Decontamination Methods.Current microbiology · 2020Review
- Mechanism and resistance for antimycobacterial activity of a fluoroquinophenoxazine compound.PloS one · 2019Article
- Microbial oil production from solid-state fermentation by a newly isolated oleaginous fungus,Royal Society open science · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacteria contain an outer membrane of unusually low permeability which contributes to their intrinsic resistance to many agents. It is assumed that small and hydrophilic antibiotics cross the outer membrane via porins, whereas hydrophobic antibiotics may diffuse through the membrane directly. A mutant of Mycobacterium smegmatis lacking the major porin MspA was used to examine the role of the porin pathway in antibiotic sensitivity. Deletion of the mspA gene caused high-level resistance of M. smegmatis to 256 microg of ampicillin/ml by increasing the MIC 16-fold. The permeation of cephaloridine in the mspA mutant was reduced ninefold, and the resistance increased eightfold. This established a clear relationship between the activity and the outer membrane permeation of cephaloridine. Surprisingly, the MICs of the large and/or hydrophobic antibiotics vancomycin, erythromycin, and rifampin for the mspA mutant were increased 2- to 10-fold. This is in contrast to those for Escherichia coli, whose sensitivity to these agents was not affected by deletion of porin genes. Uptake of the very hydrophobic steroid chenodeoxycholate by the mspA mutant was retarded threefold, which supports the hypothesis that loss of MspA indirectly reduces the permeability by the lipid pathway. The multidrug resistance of the mspA mutant highlights the prominent role of outer membrane permeability for the sensitivity of M. smegmatis to antibiotics. An understanding of the pathways across the outer membrane is essential to the successful design of chemotherapeutic agents with activities against mycobacteria.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.