Evidence map›Paper›PMID 25517613›Full record

ArticleImmunity2014

Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.

Elena Kudryashova, Royston Quintyn, Stephanie Seveau, Wuyuan Lu, Vicki H Wysocki, Dmitri S Kudryashov

Open access · bronzeAbstract read
In one paragraph

Article in Immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
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  5. The role of glycosylated mucins in maintaining intestinal homeostasis and gut health.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2025
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  8. Article
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  10. Review
  11. Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024
    Article
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  14. Stabilization of F-actin bybioRxiv : the preprint server for biology · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. A Toll pathway effector protectsProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Elena KudryashovaDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Royston QuintynDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Stephanie SeveauDepartment of Microbiology, The Ohio State University, Columbus, OH 43210, USA; Department of Microbial Infection and Immunity, The Ohio State University, Columbus, OH 43210, USA.
Wuyuan LuInstitute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Dmitri S KudryashovDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. Electronic address: kudryashov.1@osu.edu.
The Ohio State University · USUniversity of Maryland, Baltimore · US

Funding

Inhibition of Anthrax Lethal Factor by alpha-defensinsR01AI072732 · NIAID · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI LU, WUYUAN · 2007 to 2011
$2.4M
Multifaceted activity of listeriolysin O during host cell invasion by ListeriaR01AI107250 · NIAID · OHIO STATE UNIVERSITY · PI SEVEAU, STEPHANIE M M · 2014 to 2018
$1.9M
NIAID NIH HHS AI072732NIAID NIH HHS R01 AI072732NIAID NIH HHS R01 AI107250PHS HHS R01NIAID107250
6 · The paper itself

Abstract

Defensins are short cationic, amphiphilic, cysteine-rich peptides that constitute the front-line immune defense against various pathogens. In addition to exerting direct antibacterial activities, defensins inactivate several classes of unrelated bacterial exotoxins. To date, no coherent mechanism has been proposed to explain defensins' enigmatic efficiency toward various toxins. In this study, we showed that binding of neutrophil ?-defensin HNP1 to affected bacterial toxins caused their local unfolding, potentiated their thermal melting and precipitation, exposed new regions for proteolysis, and increased susceptibility to collisional quenchers without causing similar effects on tested mammalian structural and enzymatic proteins. Enteric ?-defensin HD5 and ?-defensin hBD2 shared similar toxin-unfolding effects with HNP1, albeit to different degrees. We propose that protein susceptibility to inactivation by defensins is contingent to their thermolability and conformational plasticity and that defensin-induced unfolding is a key element in the general mechanism of toxin inactivation by human defensins.

Indexed as

alpha-DefensinsAntigens, BacterialBacterial ProteinsBacterial Toxinsbeta-DefensinsCell LineChymotrypsinEnterotoxinsExotoxinsHumansProtein BindingProtein ConformationProtein UnfoldingProteolysisRepressor ProteinsThermolysinalpha-Defensinsanthrax toxinAntigens, BacterialBacterial ProteinsBacterial Toxinsbeta-DefensinsChymotrypsinDEFA5 protein, humanDEFB4A protein, humanEnterotoxinsExotoxinshuman neutrophil peptide 1Repressor ProteinsRtxA protein, Vibrio choleraetcdA protein, Clostridium difficileTcdC protein, Clostridium difficileThermolysin

Identifiers

PMID25517613
PMCPMC4269836
OpenAlexW2040297582

What OpenQuestion holds

Textmetadata
LicenceTDM
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.