Evidence map›Paper›PMID 28946740›Full record

ArticleACS synthetic biology2018

A Modular Receptor Platform To Expand the Sensing Repertoire of Bacteria.

Hung-Ju Chang, Pauline Mayonove, Agustin Zavala, Angelique De Visch, Philippe Minard, Martin Cohen-Gonsaud, Jerome Bonnet

Open access · hybridAbstract read
In one paragraph

Article in ACS synthetic biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.5field-weighted citation impact, top 10% 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, 75 citations in OpenAlex.

  1. Article
  2. Programming Next-Generation Synthetic Biosensors by Genetic Circuit Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  13. A molecular toolkit for heterologous protein secretion acrossbioRxiv : the preprint server for biology · 2023
    Article
  14. Rational design of small-molecule responsive protein switches.Protein science : a publication of the Protein Society · 2023
    Review
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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

7 authors at 2 institutions in 1 country.

Hung-Ju ChangCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.
Pauline MayonoveCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.
Agustin ZavalaCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.
Angelique De VischCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.
Philippe MinardInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay , 91191 Gif-sur-Yvette, France.
Martin Cohen-GonsaudCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.
Jerome BonnetCentre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, University of Montpellier , 34090 Montpellier, France.ORCID 0000-0002-8420-9359
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered bacteria promise to revolutionize diagnostics and therapeutics, yet many applications are precluded by the limited number of detectable signals. Here we present a general framework to engineer synthetic receptors enabling bacterial cells to respond to novel ligands. These receptors are activated via ligand-induced dimerization of a single-domain antibody fused to monomeric DNA-binding domains (split-DBDs). Using E. coli as a model system, we engineer both transmembrane and cytosolic receptors using a VHH for ligand detection and demonstrate the scalability of our platform by using the DBDs of two different transcriptional regulators. We provide a method to optimize receptor behavior by finely tuning protein expression levels and optimizing interdomain linker regions. Finally, we show that these receptors can be connected to downstream synthetic gene circuits for further signal processing. The general nature of the split-DBD principle and the versatility of antibody-based detection should support the deployment of these receptors into various hosts to detect ligands for which no receptor is found in nature.

Indexed as

Bacterial ProteinsCaffeineCell WallEscherichia coliEscherichia coli ProteinsGene ExpressionGenetic EngineeringLexA Repressor ProteinPlasmidsPromoter Regions, GeneticProtein DomainsReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsSerine EndopeptidasesSingle-Domain AntibodiesTrans-ActivatorsBacterial ProteinsCadC protein, E coliCaffeineEscherichia coli ProteinsLexA Repressor ProteinReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsSerine EndopeptidasesSingle-Domain AntibodiesTrans-Activators

Identifiers

PMID28946740
PMCPMC5880506
OpenAlexW2757646744

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.