ArticleCommunications biology2024
Sequence-structure-function characterization of the emerging tetracycline destructase family of antibiotic resistance enzymes.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 7 citations in OpenAlex.
- Evolution, Mechanisms, and Therapeutic Implications of Mobile Tetracycline Destructases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- The FAD-Dependent Monooxygenase Albo65 Mediates Self-Resistance in Albofungin Biosynthesis.JACS Au · 2026Article
- Phylogenetic Relationships and Structural Conservation ofInternational journal of molecular sciences · 2026Article
- A One Health Approach Reveals Farms as Hotspots for Co-Occurrence ofInfection and drug resistance · 2026Article
- Cooperative antibiotic resistance in bacteria: beyond biofilms.Frontiers in microbiology · 2026Review
- Binding assays enable discovery of Tet(X) inhibitors that combat tetracycline destructase resistance.Chemical science · 2025Article
- Effective simultaneous removal of 17β-estradiol and tetracycline by a novel Alkalibacterium strain: characteristics, mechanisms, and application in livestock wastewater treatment.Applied microbiology and biotechnology · 2025Article
- C10-Benzoate Esters of Anhydrotetracycline Inhibit Tetracycline Destructases and Recover Tetracycline Antibacterial Activity.ACS infectious diseases · 2025Article
- The tetracycline resistome is shaped by selection for specific resistance mechanisms by each antibiotic generation.Nature communications · 2025Article
- Multidrug-resistantFrontiers in microbiology · 2025Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Tetracycline destructases (TDases) are flavin monooxygenases which can confer resistance to all generations of tetracycline antibiotics. The recent increase in the number and diversity of reported TDase sequences enables a deep investigation of the TDase sequence-structure-function landscape. Here, we evaluate the sequence determinants of TDase function through two complementary approaches: (1) constructing profile hidden Markov models to predict new TDases, and (2) using multiple sequence alignments to identify conserved positions important to protein function. Using the HMM-based approach we screened 50 high-scoring candidate sequences in Escherichia coli, leading to the discovery of 13 new TDases. The X-ray crystal structures of two new enzymes from Legionella species were determined, and the ability of anhydrotetracycline to inhibit their tetracycline-inactivating activity was confirmed. Using the MSA-based approach we identified 31 amino acid positions 100% conserved across all known TDase sequences. The roles of these positions were analyzed by alanine-scanning mutagenesis in two TDases, to study the impact on cell and in vitro activity, structure, and stability. These results expand the diversity of TDase sequences and provide valuable insights into the roles of important residues in TDases, and flavin monooxygenases more broadly.
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Registered trials
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.