Evidence map›Paper›PMID 28764966›Full record

ArticlePeptides2017

Cathelicidins display conserved direct antiviral activity towards rhinovirus.

Filipa Henderson Sousa, Victor Casanova, Fern Findlay, Craig Stevens, Pavel Svoboda, Jan Pohl, Lorna Proudfoot, Peter G Barlow

Open access · hybridAbstract read
In one paragraph

Article in Peptides, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 92 citations in OpenAlex.

  1. Trial
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  3. Vitamin D-Induced Antimicrobial Peptides in Combating Viral Infections.Advances in experimental medicine and biology · 2026
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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 2 institutions in 2 countries.

Filipa Henderson SousaSchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom.
Victor CasanovaSchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom.
Fern FindlaySchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom.
Craig StevensSchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom.
Pavel SvobodaBiotechnology Core Facility Branch, Division of Scientific Resources, US Centers for Disease Control and Prevention, Atlanta, GA 30333, United States.
Jan PohlBiotechnology Core Facility Branch, Division of Scientific Resources, US Centers for Disease Control and Prevention, Atlanta, GA 30333, United States.
Lorna ProudfootSchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom.
Peter G BarlowSchool of Applied Sciences, Edinburgh Napier University, Sighthill Campus, Edinburgh EH11 4BN, United Kingdom. Electronic address: p.barlow@napier.ac.uk.
Edinburgh Napier University · GBCenters for Disease Control and Prevention · US

Funding

Chief Scientist Office ETM/389
6 · The paper itself

Abstract

Human rhinoviruses (HRVs) are the most common cause of viral respiratory tract infections, and are associated with significant morbidity and mortality in immunocompromised individuals and patients with pre-existing pulmonary conditions. The therapeutic options available are extremely limited and therefore novel therapeutics for HRV infections are of significant interest. Cathelicidins have been shown to have potent antiviral activity against a range of pathogens and are known to be key immunomodulatory mediators during infection. We therefore assessed the antiviral potential of cathelicidins from humans and other mammalian species against HRV, together with the potential for the human cathelicidin to modulate apoptotic pathways and alter cell viability during HRV infection. We demonstrate that LL-37, the porcine cathelicidin Protegrin-1, and the ovine cathelicidin SMAP-29 display potent antiviral activity towards HRV and that this activity is visible when either the virus is exposed to the peptides prior to cell infection or after cells have been infected. We further demonstrate that, in contrast to established findings with bacterial infection models, LL-37 does not induce apoptosis or necrosis in HRV-infected lung epithelial cells at physiological or superphysiological concentrations, but does reduce the metabolic activity of infected cells compared to uninfected cells treated with similar peptide concentrations. Collectively, the findings from this study demonstrate that the mechanism of action of cathelicidins against rhinovirus is by directly affecting the virus and we propose that the delivery of exogenous cathelicidins, or novel synthetic analogues, represent an exciting and novel therapeutic strategy for rhinovirus infection.

Indexed as

AnimalsAntimicrobial Cationic PeptidesAntiviral AgentsBlood ProteinsCathelicidinsEpithelial CellsHumansRespiratory Tract InfectionsRhinovirusSheepSwineAntimicrobial Cationic PeptidesAntiviral AgentsBlood ProteinsCathelicidinsSMAP29 protein, Ovis ariesCathelicidinInfectionLL-37RespiratoryRhinovirus

Identifiers

PMID28764966
PMCPMC5577862
OpenAlexW2740521160

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.