Evidence map›Paper›PMID 30808760›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Paneth cell α-defensins HD-5 and HD-6 display differential degradation into active antimicrobial fragments.

D Ehmann, J Wendler, L Koeninger, I S Larsen, T Klag, J Berger, A Marette, M Schaller, E F Stange, N P Malek and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
8.6field-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

64 citing papers in PubMed, 107 citations in OpenAlex.

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  16. EMC3 is critical for CFTR function and calcium mobilization in the mouse intestinal epithelium.American journal of physiology. Gastrointestinal and liver physiology · 2025
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4 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

12 authors at 3 institutions in 3 countries.

D EhmannInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
J WendlerInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
L KoeningerInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
I S LarsenQuebec Heart and Lung Institute, Department of Medicine, Faculty of Medicine, Cardiology Axis, Laval University, G1V 4G5 Quebec, QC, Canada.
T KlagInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
J BergerElectron Microscopy Unit, Max-Planck-Institute for Developmental Biology, 72076 Tübingen, Germany.
A MaretteQuebec Heart and Lung Institute, Department of Medicine, Faculty of Medicine, Cardiology Axis, Laval University, G1V 4G5 Quebec, QC, Canada.
M SchallerDepartment of Dermatology, University Hospital Tübingen, 72076 Tübingen, Germany.
E F StangeInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
N P MalekInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany.
B A H JensenQuebec Heart and Lung Institute, Department of Medicine, Faculty of Medicine, Cardiology Axis, Laval University, G1V 4G5 Quebec, QC, Canada.
J WehkampInternal Medicine I, University Hospital Tübingen, 72076 Tübingen, Germany; jan.wehkamp@med.uni-tuebingen.de.
University Children's Hospital Tübingen · DEUniversité Laval · CAMax Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides, in particular α-defensins expressed by Paneth cells, control microbiota composition and play a key role in intestinal barrier function and homeostasis. Dynamic conditions in the local microenvironment, such as pH and redox potential, significantly affect the antimicrobial spectrum. In contrast to oxidized peptides, some reduced defensins exhibit increased vulnerability to proteolytic degradation. In this report, we investigated the susceptibility of Paneth-cell-specific human α-defensin 5 (HD-5) and -6 (HD-6) to intestinal proteases using natural human duodenal fluid. We systematically assessed proteolytic degradation using liquid chromatography-mass spectrometry and identified several active defensin fragments capable of impacting bacterial growth of both commensal and pathogenic origins. Of note, incubation of mucus with HD-5 resulted in 255-8,000 new antimicrobial combinations. In contrast, HD-6 remained stable with consistent preserved nanonet formation. In vivo studies demonstrated proof of concept that a HD-5 fragment shifted microbiota composition (e.g., increases of

Indexed as

alpha-DefensinsAnimalsAnti-Infective AgentsCellular MicroenvironmentHost Microbial InteractionsHumansHydrogen-Ion ConcentrationIntestinal MucosaMiceMicrobiotaOxidation-ReductionPaneth CellsPeptidesProteolysisalpha-DefensinsAnti-Infective AgentsDEFA5 protein, humanDEFA6 protein, humanPeptidesantimicrobial peptideshost–microbiota interactionintestinal barrierproteolytic digestionα-defensins

Identifiers

PMID30808760
PMCPMC6397583
OpenAlexW2914417447

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.