Evidence map›Paper›PMID 22780862›Full record

ArticleMolecular microbiology2012

Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal.

Luis Alberto Vega, Michael G Caparon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Strain-Specific Adaptations ofAntibiotics (Basel, Switzerland) · 2020
    Article
  14. Sub-inhibitory Effects of Antimicrobial Peptides.Frontiers in microbiology · 2019
    Review
  15. Review
  16. Article
  17. Guardians of the Gut: Enteric Defensins.Frontiers in microbiology · 2017
    Review
  18. Polymyxin: Alternative Mechanisms of Action and Resistance.Cold Spring Harbor perspectives in medicine · 2016
    Review
  19. Antimicrobial Peptides Targeting Gram-Positive Bacteria.Pharmaceuticals (Basel, Switzerland) · 2016
    Review
  20. Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides.Frontiers in cell and developmental biology · 2016
    Review
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

2 authors at 1 institution in 1 country.

Luis Alberto VegaDepartment of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63110-1093, USA.
Michael G Caparon
Washington University in St. Louis · US

Funding

PROTEASE AND ROP GENES IN S. PYOGENES VIRULENCER01AI046433 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2000 to 2014
$4.7M
Characterizing Exportal by a Polymyxin B Resistance-Based Mutagenic ApproachF31AI081504 · NIAID · WASHINGTON UNIVERSITY · PI VEGA, LUIS ALBERTO · 2009 to 2010
$56k
NIAID NIH HHS 1F31AI081504-01A1NIAID NIH HHS AI46433NIAID NIH HHS F31 AI081504NIAID NIH HHS R01 AI046433
6 · The paper itself

Abstract

Although they possess a well-characterized ability to porate the bacterial membrane, emerging research suggests that cationic antimicrobial peptides (CAPs) can influence pathogen behaviour at levels that are sublethal. In this study, we investigated the interaction of polymyxin B and human neutrophil peptide (HNP-1) with the human pathogen Streptococcus pyogenes. At sublethal concentrations, these CAPs preferentially targeted the ExPortal, a unique microdomain of the S. pyogenes membrane, specialized for protein secretion and processing. A consequence of this interaction was the disruption of ExPortal organization and a redistribution of ExPortal components into the peripheral membrane. Redistribution was associated with inhibition of secretion of certain toxins, including the SpeB cysteine protease and the streptolysin O (SLO) cytolysin, but not SIC, a protein that protects S. pyogenes from CAPs. These data suggest a novel function for CAPs in targeting the ExPortal and interfering with secretion of factors required for infection and survival. This mechanism may prove valuable for the design of new types of antimicrobial agents to combat the emergence of antibiotic-resistant pathogens.

Indexed as

alpha-DefensinsAntimicrobial Cationic PeptidesHumansMembrane Transport ProteinsPolymyxin BStreptococcus pyogenesVirulence Factorsalpha-DefensinsAntimicrobial Cationic Peptideshuman neutrophil peptide 1Membrane Transport ProteinsPolymyxin BVirulence Factors

Identifiers

PMID22780862
PMCPMC3646575
OpenAlexW2107070502

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.