ArticleAntimicrobial agents and chemotherapy2012
Characterization of a rifampin-inactivating glycosyltransferase from a screen of environmental actinomycetes.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Ngt-1: A glycosyltransferase that confers resistance to three distinct antibiotic classes.The Journal of biological chemistry · 2026Article
- The bacterial phosphotransferase system-mediated rifampicin phosphorylation: ancestral links to rifampicin-inactivating enzyme.Frontiers in microbiology · 2026Article
- Panoramic description of ROS-based nanotechnology for osteomyelitis therapy: Challenges, opportunities, and prospects.Theranostics · 2026Review
- Unveiling the Mechanisms of Bacterial Resistance and Countermeasures.Pathogens (Basel, Switzerland) · 2025Review
- Acquired Bacterial Resistance to Antibiotics and Resistance Genes: From Past to Future.Antibiotics (Basel, Switzerland) · 2025Review
- Recent Advances in Antimicrobial Resistance: Insights fromMicroorganisms · 2024Review
- Characterization of the soil resistome and mobilome in Namib Desert soils.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Molecular mechanisms of antibiotic resistance revisited.Nature reviews. Microbiology · 2023Review
- The role of adjuvants in overcoming antibacterial resistance due to enzymatic drug modification.RSC medicinal chemistry · 2022Review
- C25-modified rifamycin derivatives with improved activity againstPNAS nexus · 2022Article
- Activation of the SigE-SigB signaling pathway by inhibition of the respiratory electron transport chain and its effect on rifampicin resistance in Mycobacterium smegmatis.Journal of microbiology (Seoul, Korea) · 2022Article
- Antimicrobial Susceptibility of Clinical Oral Isolates ofMicroorganisms · 2022Article
- Kanglemycin A Can Overcome Rifamycin Resistance Caused by ADP-Ribosylation by Arr Protein.Antimicrobial agents and chemotherapy · 2021Article
- Rifamycin antibiotics and the mechanisms of their failure.The Journal of antibiotics · 2021Review
- Antibiotic resistome from the One-Health perspective: understanding and controlling antimicrobial resistance transmission.Experimental & molecular medicine · 2021Review
- Characterization of the Rifamycin-Degrading Monooxygenase From Rifamycin Producers Implicating Its Involvement in Saliniketal Biosynthesis.Frontiers in microbiology · 2020Article
- Antibiotic resistance genes in the Actinobacteria phylum.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2019Review
- Repositioning rifamycins for Mycobacterium abscessus lung disease.Expert opinion on drug discovery · 2019Review
- Crossroads of Antibiotic Resistance and Biosynthesis.Journal of molecular biology · 2019Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides insight into the evolution of antibiotic resistance and critical information for the development of future antimicrobials. The rifamycins are broad-spectrum antibiotics that target bacterial transcription by inhibition of RNA polymerase. Although mutational alteration of the drug target is the predominant mechanism of resistance to this family of antibiotics in the clinic, a number of diverse inactivation mechanisms have also been reported. In this report, we investigate a subset of environmental rifampin-resistant actinomycete isolates and identify a diverse collection of rifampin inactivation mechanisms. We describe a single isolate, WAC1438, capable of inactivating rifampin by glycosylation. A draft genome sequence of WAC1438 (most closely related to Streptomyces speibonae, according to a 16S rRNA gene comparison) was assembled, and the associated rifampin glycosyltransferase open reading frame, rgt1438, was identified. The role of rgt1438 in rifampin resistance was confirmed by its disruption in the bacterial chromosome, resulting in a loss of antibiotic inactivation and a 4-fold decrease in MIC. Interestingly, examination of the RNA polymerase β-subunit sequence of WAC1438 suggests that it harbors a resistant target and thus possesses dual mechanisms of rifamycin resistance. Using an in vitro assay with purified enzyme, Rgt1438 could inactivate a variety of rifamycin antibiotics with comparable steady-state kinetics constants. Our results identify rgt1438 as a rifampin resistance determinant from WAC1438 capable of inactivating an assortment of rifamycins, adding a new element to the rifampin resistome.
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