Evidence map›Paper›PMID 25927541›Full record

ArticleACS nano2015

Using surface enhanced Raman scattering to analyze the interactions of protein receptors with bacterial quorum sensing modulators.

Celina Costas, Vanesa López-Puente, Gustavo Bodelón, Concepción González-Bello, Jorge Pérez-Juste, Isabel Pastoriza-Santos, Luis M Liz-Marzán

Abstract read
In one paragraph

Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Anti-quorum sensing activity ofBioinformation · 2023
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Surface-Enhanced Raman Scattering Spectroscopy for Label-Free Analysis ofFrontiers in cellular and infection microbiology · 2018
    Review
  12. Article
  13. Ultrasensitive surface-enhanced Raman scattering detection in common fluids.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
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.

Celina Costas†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.
Vanesa López-Puente†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.
Gustavo Bodelón†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.
Concepción González-Bello‡Centro Singular de Investigación en Química Biológica y Materiales Moleculares (CIQUS), Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain.
Jorge Pérez-Juste†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.
Isabel Pastoriza-Santos†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.
Luis M Liz-Marzán†Departamento de Química Física, Universidade de Vigo, 36301 Vigo, Spain.

Funding

European Research Council 267867
6 · The paper itself

Abstract

Many members of the LuxR family of quorum sensing (QS) transcriptional activators, including LasR of Pseudomonas aeruginosa, are believed to require appropriate acyl-homoserine lactone (acyl-HSL) ligands to fold into an active conformation. The failure to purify ligand-free LuxR homologues in nonaggregated form at the high concentrations required for their structural characterization has limited the understanding of the mechanisms by which QS receptors are activated. Surface-enhanced Raman scattering (SERS) is a vibrational spectroscopy technique that can be applied to study proteins at extremely low concentrations in their active state. The high sensitivity of SERS has allowed us to detect molecular interactions between the ligand-binding domain of LasR (LasRLBD) as a soluble apoprotein and modulators of P. aeruginosa QS. We found that QS activators and inhibitors produce differential SERS fingerprints in LasRLBD, and in combination with molecular docking analysis provide insight into the relevant interaction mechanism. This study reveals signal-specific structural changes in LasR upon ligand binding, thereby confirming the applicability of SERS to analyze ligand-induced conformational changes in proteins.

Indexed as

Quorum SensingSpectrum Analysis, RamanApoproteinsBacterial ProteinsGoldLigandsMolecular Docking SimulationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryPseudomonas aeruginosaSurface PropertiesTrans-ActivatorsApoproteinsBacterial ProteinsGoldLasR protein, Pseudomonas aeruginosaLigandsTrans-Activatorsnanoplasmonicsprotein receptorsPseudomonas aeruginosaquorum sensingSERS

Identifiers

PMID25927541
PMCPMC4446724

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.