ArticleJournal of bacteriology2011
Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes Bacteria.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 157 citations in OpenAlex.
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- The extracellular domain ofFrontiers in microbiology · 2025Article
- Guarding the walls: the multifaceted roles of Bce modules in cell envelope stress sensing and antimicrobial resistance.Journal of bacteriology · 2024Review
- HssS activation by membrane heme defines a paradigm for two-component system signaling inmBio · 2024Article
- Perception and protection: The role of Bce-modules in antimicrobial peptide resistance.Biochimica et biophysica acta. Biomembranes · 2024Review
- Cross-regulation of Aps-promoters in Lacticaseibacillus paracasei by the PsdR response regulator in response to lantibiotics.Scientific reports · 2024Article
- Daptomycin avoids drug resistance mediated by the BceAB transporter inMicrobiology spectrum · 2024Article
- Membrane Lipids Augment Cell Envelope Stress Signaling and Resistance to Antibiotics and Antimicrobial Peptides inbioRxiv : the preprint server for biology · 2023Article
- Architecture of a complete Bce-type antimicrobial peptide resistance module.Nature communications · 2023Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Correlations among Antibiotic Resistance Genes, Mobile Genetic Elements and Microbial Communities in Municipal Sewage Treatment Plants Revealed by High-Throughput Sequencing.International journal of environmental research and public health · 2023Article
- Association of Midgut Bacteria and Their Metabolic Pathways with Zika Infection and Insecticide Resistance in ColombianViruses · 2022Article
- Toward the Complete Functional Characterization of a Minimal Bacterial Proteome.The journal of physical chemistry. B · 2022Article
- Comparative genome analysis of Vagococcus fluvialis reveals abundance of mobile genetic elements in sponge-isolated strains.BMC genomics · 2022Article
26 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Firmicutes bacteria, ATP-binding cassette (ABC) transporters have been recognized as important resistance determinants against antimicrobial peptides. Together with neighboring two-component systems (TCSs), which regulate their expression, they form specific detoxification modules. Both the transport permease and sensor kinase components show unusual domain architecture: the permeases contain a large extracellular domain, while the sensor kinases lack an obvious input domain. One of the best-characterized examples is the bacitracin resistance module BceRS-BceAB of Bacillus subtilis. Strikingly, in this system, the ABC transporter and TCS have an absolute mutual requirement for each other in both sensing of and resistance to bacitracin, suggesting a novel mode of signal transduction in which the transporter constitutes the actual sensor. We identified over 250 such BceAB-like ABC transporters in the current databases. They occurred almost exclusively in Firmicutes bacteria, and 80% of the transporters were associated with a BceRS-like TCS. Phylogenetic analyses of the permease and sensor kinase components revealed a tight evolutionary correlation. Our findings suggest a direct regulatory interaction between the ABC transporters and TCSs, mediating communication between both components. Based on their observed coclustering and conservation of response regulator binding sites, we could identify putative corresponding two-component systems for transporters lacking a regulatory system in their immediate neighborhood. Taken together, our results show that these types of ABC transporters and TCSs have coevolved to form self-sufficient detoxification modules against antimicrobial peptides, widely distributed among Firmicutes bacteria.
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