ArticleProceedings of the National Academy of Sciences of the United States of America2013
Transcriptomic and biochemical analyses identify a family of chlorhexidine efflux proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 174 citations in OpenAlex.
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- Enzyme-Ligand Interaction Monitored by Synchrotron Radiation Circular Dichroism.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Potential of isoquinoline-alkaloid-richFrontiers in pharmacology · 2026Article
- Gramicidin and chlorhexidine encapsulated in bicontinuous microemulsions: antimicrobial activity performance and their impact on self-assembly.Journal of surfactants and detergents · 2025Article
- Plant Metabolites as Potential Agents That Potentiate or Block Resistance Mechanisms Involving β-Lactamases and Efflux Pumps.International journal of molecular sciences · 2025Review
- Metal-Based Approaches for the Fight against Antimicrobial Resistance: Mechanisms, Opportunities, and Challenges.Journal of the American Chemical Society · 2025Review
- NosocomialInternational journal of molecular sciences · 2025Article
- Integrative review on Acinetobacter baumannii as a multidrug-resistant pathogen: resistance mechanisms and therapeutic perspectives in the context of nosocomial infections.Revista da Sociedade Brasileira de Medicina Tropical · 2025Review
- Roles of mobile genetic elements and biosynthetic gene clusters in environmental adaptation of acidophilic archaeonFrontiers in microbiology · 2025Article
- Comprehensive Approaches to CombattingAntibiotics (Basel, Switzerland) · 2024Review
- Genomic insights into the adaptation of Acinetobacter johnsonii RB2-047 to the heavy metal-contaminated subsurface mine environment.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Types and Mechanisms of Efflux Pump Systems and the Potential of Efflux Pump Inhibitors in the Restoration of Antimicrobial Susceptibility, with a Special Reference toPathogens (Basel, Switzerland) · 2024Review
- Inhibition of biofilm formation and preformed biofilm inFrontiers in microbiology · 2024Article
- Systematic analyses identify modes of action of ten clinically relevant biocides and antibiotic antagonism in Acinetobacter baumannii.Nature microbiology · 2023Article
- Advances in the Discovery of Efflux Pump Inhibitors as Novel Potentiators to Control Antimicrobial-Resistant Pathogens.Antibiotics (Basel, Switzerland) · 2023Review
- Chlorhexidine Resistance or Cross-Resistance, That Is the Question.Antibiotics (Basel, Switzerland) · 2023Review
- Mechanistic insights into nanoparticle surface-bacterial membrane interactions in overcoming antibiotic resistance.Frontiers in microbiology · 2023Review
- Sterilizing orthodontic appliances: A systematic review and meta-analysis on the available methods.Journal of orthodontic science · 2023Review
- New understanding of multidrug efflux and permeation in antibiotic resistance, persistence, and heteroresistance.Annals of the New York Academy of Sciences · 2023Review
31 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlorhexidine is widely used as an antiseptic or disinfectant in both hospital and community settings. A number of bacterial species display resistance to this membrane-active biocide. We examined the transcriptomic response of a representative nosocomial human pathogen, Acinetobacter baumannii, to chlorhexidine to identify the primary chlorhexidine resistance elements. The most highly up-regulated genes encoded components of a major multidrug efflux system, AdeAB. The next most highly overexpressed gene under chlorhexidine stress was annotated as encoding a hypothetical protein, named here as AceI. Orthologs of the aceI gene are conserved within the genomes of a broad range of proteobacterial species. Expression of aceI or its orthologs from several other γ- or β-proteobacterial species in Escherichia coli resulted in significant increases in resistance to chlorhexidine. Additionally, disruption of the aceI ortholog in Acinetobacter baylyi rendered it more susceptible to chlorhexidine. The AceI protein was localized to the membrane after overexpression in E. coli. This protein was purified, and binding assays demonstrated direct and specific interactions between AceI and chlorhexidine. Transport assays using [(14)C]-chlorhexidine determined that AceI was able to mediate the energy-dependent efflux of chlorhexidine. An E15Q AceI mutant with a mutation in a conserved acidic residue, although unable to mediate chlorhexidine resistance and transport, was still able to bind chlorhexidine. Taken together, these data are consistent with AceI being an active chlorhexidine efflux protein and the founding member of a family of bacterial drug efflux transporters.
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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.