ArticleApplied and environmental microbiology2010
AidH, an alpha/beta-hydrolase fold family member from an Ochrobactrum sp. strain, is a novel N-acylhomoserine lactonase.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 107 citations in OpenAlex.
- In silico identification of novel alpha/beta hydrolase fold domain-containing protein associated with virulence and antibiotic resistance in Nocardia farcinica (Strain: JJSBBCNF_01).Molecular diversity · 2026Article
- Targeting biofilm and virulence inMicrobiology spectrum · 2026Article
- Quorum quenching pathoblockers from bacteria: an alternative approach for bacterial infection management.Folia microbiologica · 2026Review
- Responses of rumen bacterial microflora to aflatoxin B1 challenge: potential roles of AHLs/AI-2 mediated quorum sensing.Animal microbiome · 2026Article
- Quorum-quenching for bacterial pathogen control and health management in aquaculture: mechanisms, applications, current status and future prospects.Frontiers in systems biology · 2026Review
- Next-generation anti-infective drugs in the post-antibiotic era: focusing on anti-virulence agents targeting the bacterial quorum sensing system.Frontiers in cellular and infection microbiology · 2026Review
- A Novel Screening System to Characterize and Engineer Quorum Quenching Lactonases.Biotechnology and bioengineering · 2025Article
- Targeting quorum sensing for manipulation of commensal microbiota.BMC biotechnology · 2024Review
- MzmL, a novel marine derivedFrontiers in microbiology · 2024Article
- Targeting Multidrug-Recalcitrant Pseudomonas aeruginosa Biofilms: Combined-Enzyme Treatment Enhances Antibiotic Efficacy.Antimicrobial agents and chemotherapy · 2023Article
- A putative glucose 6-phosphate isomerase has pleiotropic functions on virulence and other mechanisms inFrontiers in plant science · 2023Article
- Innovative microbial disease biocontrol strategies mediated by quorum quenching and their multifaceted applications: A review.Frontiers in plant science · 2022Review
- Epidermal galactose spurs chytrid virulence and predicts amphibian colonization.Nature communications · 2021Article
- Pathogen Biocontrol Using Plant Growth-Promoting Bacteria (PGPR): Role of Bacterial Diversity.Microorganisms · 2021Review
- Quorum quenching enzymes and their effects on virulence, biofilm, and microbiomes: a review of recent advances.Expert review of anti-infective therapy · 2020Review
- Improving the production of AHL lactonase AiiO-AIO6 from Ochrobactrum sp. M231 in intracellular protease-deficient Bacillus subtilis.AMB Express · 2020Article
- Identification of a Second Type of AHL-lactonase fromJournal of microbiology and biotechnology · 2020Article
- Potential of a Quorum Quenching Bacteria IsolateFrontiers in microbiology · 2020Article
- AidB, a Novel ThermostableApplied and environmental microbiology · 2019Article
- Quorum Quenching Enzyme APTM01, an Acylhomoserine-Lactone Acylase from Marine Bacterium of Pseudoalteromonas tetraodonis Strain MQS005.Current microbiology · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-acylhomoserine lactones (AHLs) are signaling molecules in many quorum-sensing (QS) systems that regulate interactions between various pathogenic bacteria and their hosts. Quorum quenching by the enzymatic inactivation of AHLs holds great promise in preventing and treating infections, and several such enzymes have been reported. In this study, we report the characterization of a novel AHL-degrading protein from the soil bacterium Ochrobactrum sp. strain T63. This protein, termed AidH, shares no similarity with any of the known AHL degradases but is highly homologous with a hydrolytic enzyme from Ochrobactrum anthropi ATCC 49188 that contains the alpha/beta-hydrolase fold. By liquid chromatography-mass spectrometry (MS) analysis, we demonstrate that AidH functions as an AHL-lactonase that hydrolyzes the ester bond of the homoserine lactone ring of AHLs. Mutational analyses indicate that the G-X-Nuc-X-G motif or the histidine residue conserved among alpha/beta-hydrolases is critical for the activity of AidH. Furthermore, the AHL-inactivating activity of AidH requires Mn(2+) but not several other tested divalent cations. We also showed that AidH significantly reduces biofilm formation by Pseudomonas fluorescens 2P24 and the pathogenicity of Pectobacterium carotovorum, indicating that this enzyme is able to effectively quench QS-dependent functions in these bacteria by degrading AHLs.
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