Evidence map›Paper›PMID 32690609›Full record

ReviewThe Journal of biological chemistry2020

Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control.

Raphaël Billot, Laure Plener, Pauline Jacquet, Mikael Elias, Eric Chabrière, David Daudé

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Engineering quorum quenching acylases with improved kinetic and biochemical properties.Protein science : a publication of the Protein Society · 2024
    Article
  11. Article
  12. Quorum-quenching enzyme Est816 assisted antibiotics against periodontitis induced byFrontiers in cellular and infection microbiology · 2024
    Article
  13. Article
  14. Thermostable Lactonases InhibitInternational journal of molecular sciences · 2023
    Article
  15. Mutexa: A Computational Ecosystem for Intelligent Protein Engineering.Journal of chemical theory and computation · 2023
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Raphaël BillotGene&GreenTK, Marseille, France; IRD, APHM, MEPHI, IHU-Méditerranée Infection, Aix-Marseille Université, Marseille, France.
Laure PlenerGene&GreenTK, Marseille, France.
Pauline JacquetGene&GreenTK, Marseille, France.
Mikael EliasMolecular Biology and Biophysics and Biotechnology Institute, Department of Biochemistry, University of Minnesota, St. Paul, Minnesota, USA.
Eric ChabrièreIRD, APHM, MEPHI, IHU-Méditerranée Infection, Aix-Marseille Université, Marseille, France. Electronic address: eric.chabriere@univ-amu.fr.
David DaudéGene&GreenTK, Marseille, France. Electronic address: david.daude@gene-greentk.com.
Méditerranée Infection Foundation · FRAix-Marseille Université · FRUniversity of Minnesota · US

Funding

Unravelling the Importance of Bacterial Signaling using Specific Interference StrategiesR35GM133487 · NIGMS · UNIVERSITY OF MINNESOTA · PI Mikael H Elias · 2019 to 2026
$2.7M
NIGMS NIH HHS R35 GM133487
6 · The paper itself

Abstract

Enzymes able to degrade or modify acyl-homoserine lactones (AHLs) have drawn considerable interest for their ability to interfere with the bacterial communication process referred to as quorum sensing. Many proteobacteria use AHL to coordinate virulence and biofilm formation in a cell density-dependent manner; thus, AHL-interfering enzymes constitute new promising antimicrobial candidates. Among these, lactonases and acylases have been particularly studied. These enzymes have been isolated from various bacterial, archaeal, or eukaryotic organisms and have been evaluated for their ability to control several pathogens. Engineering studies on these enzymes were carried out and successfully modulated their capacity to interact with specific AHL, increase their catalytic activity and stability, or enhance their biotechnological potential. In this review, special attention is paid to the screening, engineering, and applications of AHL-modifying enzymes. Prospects and future opportunities are also discussed with a view to developing potent candidates for bacterial control.

Indexed as

BacteriaBacterial ProteinsCarboxylic Ester HydrolasesMetabolic EngineeringQuorum SensingAcyl-ButyrolactonesAnti-Bacterial AgentsAcyl-ButyrolactonesAnti-Bacterial AgentsBacterial ProteinsCarboxylic Ester Hydrolasesacylaseacyl-homoserine lactones quorum sensingantibiotic resistancebiofilmenzyme catalysislactonaseprotein engineeringquorum quenchingvirulence factor

Identifiers

PMID32690609
PMCPMC7489903
OpenAlexW3042556385

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.