Evidence map›Paper›PMID 28814602›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2017

Carbon Nanoparticles Inhibit the Antimicrobial Activities of the Human Cathelicidin LL-37 through Structural Alteration.

Fern Findlay, Jan Pohl, Pavel Svoboda, Priyanka Shakamuri, Kevin McLean, Neil F Inglis, Lorna Proudfoot, Peter G Barlow

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Immune Fingerprint in Diabetes: Ocular Surface and Retinal Inflammation.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Antiviral Activities of Human Host Defense Peptides.Current medicinal chemistry · 2020
    Review
  15. Article
  16. Review
  17. 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

8 authors at 3 institutions in 2 countries.

Fern FindlaySchool of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom.
Jan PohlBiotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and.
Pavel SvobodaBiotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and.
Priyanka ShakamuriBiotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and.
Kevin McLeanMoredun Proteomics Facility, Moredun Research Institute, Penicuik EH26 0PZ, United Kingdom.
Neil F InglisMoredun Proteomics Facility, Moredun Research Institute, Penicuik EH26 0PZ, United Kingdom.
Lorna ProudfootSchool of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom.ORCID 0000-0002-4042-8058
Peter G BarlowSchool of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom; p.barlow@napier.ac.uk.ORCID 0000-0002-6516-9312
Centers for Disease Control and Prevention · USEdinburgh Napier University · GBMoredun Research Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Host defense peptides, also known as antimicrobial peptides, are key elements of innate host defense. One host defense peptide with well-characterized antimicrobial activity is the human cathelicidin, LL-37. LL-37 has been shown to be upregulated at sites of infection and inflammation and is regarded as one of the primary innate defense molecules against bacterial and viral infection. Human exposure to combustion-derived or engineered nanoparticles is of increasing concern, and the implications of nanomaterial exposure on the human immune response is poorly understood. However, it is widely acknowledged that nanoparticles can interact strongly with several immune proteins of biological significance, with these interactions resulting in structural and functional changes of the proteins involved. This study investigated whether the potent antibacterial and antiviral functions of LL-37 were inhibited by exposure to, and interaction with, carbon nanoparticles, together with characterizing the nature of the interaction. LL-37 was exposed to carbon black nanoparticles in vitro, and the antibacterial and antiviral functions of the peptide were subsequently assessed. We demonstrate a substantial loss of antimicrobial function when the peptide was exposed to low concentrations of nanomaterials, and we further show that the nanomaterial-peptide interaction resulted in a significant change in the structure of the peptide. The human health implications of these findings are significant, as, to our knowledge, this is the first evidence that nanoparticles can alter host defense peptide structure and function, indicating a new role for nanoparticle exposure in increased disease susceptibility.

Indexed as

CarbonAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntiviral AgentsBacteriaCathelicidinsHumansInflammationNanoparticlesRhinovirusAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntiviral AgentsCarbonCathelicidins

Identifiers

PMID28814602
PMCPMC5602159
OpenAlexW2745851529

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.