Evidence map›Paper›PMID 26257736›Full record

ArticleFrontiers in immunology2015

Tasting Pseudomonas aeruginosa Biofilms: Human Neutrophils Express the Bitter Receptor T2R38 as Sensor for the Quorum Sensing Molecule N-(3-Oxododecanoyl)-l-Homoserine Lactone.

Susanne Maurer, Guido H Wabnitz, Nadine A Kahle, Sabine Stegmaier, Birgit Prior, Thomas Giese, Matthias Martin Gaida, Yvonne Samstag, Gertrud Maria Hänsch

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed, 1 pooled it
10.5field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 1 synthesis or guideline pooled it, 129 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
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  5. Direct Maxillary Sinus Tissue Analysis forJournal of clinical medicine · 2026
    Article
  6. Review
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  8. Article
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  11. A deadly taste: linking bitter taste receptors and apoptosis.Apoptosis : an international journal on programmed cell death · 2025
    Review
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  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Mechanisms of the Quorum Sensing Systems ofCurrent medicinal chemistry · 2024
    Review
  20. Review

21 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Susanne MaurerInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Guido H WabnitzInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Nadine A KahleInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Sabine StegmaierInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Birgit PriorInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Thomas GieseInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Matthias Martin GaidaInstitute for Immunology, University of Heidelberg , Heidelberg , Germany ; Institute of Pathology, University of Heidelberg , Heidelberg , Germany.
Yvonne SamstagInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Gertrud Maria HänschInstitute for Immunology, University of Heidelberg , Heidelberg , Germany.
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria communicate with one another via specialized signaling molecules, known as quorum sensing molecules or autoinducers. The Pseudomonas aeruginosa-derived quorum sensing molecule N-(3-oxododecanoyl)-l-homoserine lactone (AHL-12), however, also activates mammalian cells. As shown previously, AHL-12-induced chemotaxis, up-regulated CD11b expression, and enhanced phagocytosis of polymorphonuclear neutrophils. Circumstantial evidence concurred with a receptor for AHL-12, which has been elusive so far. We now investigated the bitter receptor T2R38 as a potential candidate. Although identified as a taste receptor, extragustatory cells express T2R38, for example, epithelial cells in the lung. We now detected T2R38 in peripheral blood neutrophils, monocytes, and lymphocytes. T2R38 is not only found on the cell membrane but also intracellular. In neutrophils, T2R38 was located in vesicles with characteristics of lipid droplets, and super-resolution microscopy showed a co-localization with the lipid droplet membrane. Neutrophils take up AHL-12, and it co-localized with T2R38 as seen by laser scan microscopy. Binding of AHL-12 to T2R28 was confirmed by pull-down assays using biotin-coupled AHL-12 as bait. A commercially available antibody to T2R38 inhibited binding of AHL-12 to neutrophils, and this antibody by itself stimulated neutrophils, similarly to AHL-12. In conclusion, our data provide evidence for expression of functional T2R38 on neutrophils, and are compatible with the notion that T2R38 is the receptor for AHL-12.

Indexed as

bitter receptor T2R38lipid dropletsN-(3-oxododecanoyl)-l-homoserine lactoneneutrophilsPseudomonas aeruginosaquorum sensing

Identifiers

PMID26257736
PMCPMC4513437
OpenAlexW1598738229

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.