ArticleMicrobial biotechnology2010
Characterization of the RND family of multidrug efflux pumps: in silico to in vivo confirmation of four functionally distinct subgroups.
Article in Microbial biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 42 citations in OpenAlex.
- Development of advanced bioinformatic profiles to improve the detection and functional understanding of fungal acid phosphatases.Applied and environmental microbiology · 2026Article
- Mutations in ribosomal protein uS5 alter translation fidelity and mutagenesis inJournal of bacteriology · 2025Article
- Unraveling the genomic diversity of the Pseudomonas putida group: exploring taxonomy, core pangenome, and antibiotic resistance mechanisms.FEMS microbiology reviews · 2024Review
- Antibiotic Resistance in Acetic Acid Bacteria Originating from Vinegar.Antibiotics (Basel, Switzerland) · 2024Article
- HME, NFE, and HAE-1 efflux pumps in Gram-negative bacteria: a comprehensive phylogenetic and ecological approach.ISME communications · 2024Article
- Adaptive laboratory evolution ofMetabolic engineering communications · 2020Article
- Co-occurrence of antibiotic, biocide, and heavy metal resistance genes in bacteria from metal and radionuclide contaminated soils at the Savannah River Site.Microbial biotechnology · 2020Article
- Resistance to Bipyridyls Mediated by the TtgABC Efflux System inFrontiers in microbiology · 2020Article
- Phylogenetic analysis reveals an ancient gene duplication as the origin of the MdtABC efflux pump.PloS one · 2020Article
- The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Clinical microbiology reviews · 2015Review
- Correlation between AcrB trimer association affinity and efflux activity.Biochemistry · 2014Article
- Bactericidal and bacteriostatic antibiotics and the Fenton reaction.Microbial biotechnology · 2014Article
- Antibiotic resistance determinants in a Pseudomonas putida strain isolated from a hospital.PloS one · 2014Article
- Metabolic potential of the organic-solvent tolerant Pseudomonas putida DOT-T1E deduced from its annotated genome.Microbial biotechnology · 2013Article
- Mechanisms of resistance to chloramphenicol in Pseudomonas putida KT2440.Antimicrobial agents and chemotherapy · 2012Article
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Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed a generalized profile that identifies members of the root-nodulation-cell-division (RND) family of efflux pumps and classifies them into four functional subfamilies. According to Z-score values, efflux pumps can be grouped by their metabolic function, thus making it possible to distinguish pumps involved in antibiotic resistance (group 1) from those involved in metal resistance (group 3). In silico data regarding efflux pumps in group 1 were validated after identification of RND efflux pumps in a number of environmental microbes that were isolated as resistant to ethidium bromide. Analysis of the Pseudomonas putida KT2440 genome identified efflux pumps in all groups. A collection of mutants in efflux pumps and a screening platform consisting of 50 drugs were created to assign a function to the efflux pumps. We validated in silico data regarding efflux pumps in groups 1 and 3 using 9 different mutants. Four mutants belonging to group 2 were found to be more sensitive than the wild-type to oxidative stress-inducing agents such as bipyridyl and methyl viologen. The two remaining mutants belonging to group 4 were found to be more sensitive than the parental to tetracycline and one of them was particularly sensitive to rubidium and chromate. By effectively combining in vivo data with generalized profiles and gene annotation data, this approach allowed the assignment, according to metabolic function, of both known and uncharacterized RND efflux pumps into subgroups, thereby providing important new insight into the functions of proteins within this family.
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