Evidence map›Paper›PMID 30462698›Full record

ArticlePloS one2018

Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide.

Somia Debbabi, Marie-Christine Groleau, Myriam Létourneau, Chitra Narayanan, Laura-Lee Gosselin, Mustapha Iddir, Jacinthe Gagnon, Nicolas Doucet, Eric Déziel, David Chatenet

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. An ancient neuropeptide defends the brain against infection.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. Neuropeptides in gut-brain axis and their influence on host immunity and stress.Computational and structural biotechnology journal · 2020
    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

10 authors at 1 institution in 1 country.

Somia DebbabiINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Marie-Christine GroleauINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.ORCID 0000-0003-4810-1030
Myriam LétourneauINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Chitra NarayananINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Laura-Lee GosselinINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Mustapha IddirINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Jacinthe GagnonINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Nicolas DoucetINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
Eric DézielINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
David ChatenetINRS-Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.ORCID 0000-0002-7270-4328
Institut National de la Recherche Scientifique · CA

Funding

Conformational sub-states in enzyme catalysis: Applications to ribonucleaseR01GM105978 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AGARWAL, PRATUL K, CHENNUBHOTLA, SRINIVAS CHAKRA · 2014 to 2018
$2.8M
NIGMS NIH HHS R01 GM105978
6 · The paper itself

Abstract

The Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP), a polycationic, amphiphilic and helical neuropeptide, is well known for its neuroprotective actions and cell penetrating properties. In the present study, we evaluated the potent antibacterial property of PACAP38 and related analogs against various bacterial strains. Interestingly, PACAP38 and related analogs can inhibit the growth of various bacteria including Escherichia coli (JM109), Bacillus subtilis (PY79), and the pathogenic Burkholderia cenocepacia (J2315). Investigation of the mechanism of action suggested that a PACAP metabolite, identified as PACAP(9-38), might indeed be responsible for the observed PACAP38 antibacterial action. Surprisingly, PACAP(9-38), which does not induce haemolysis, exhibits an increased specificity toward Burkholderia cenocepacia J2315 compared to other tested bacteria. Finally, the predisposition of PACAP(9-38) to adopt a π-helix conformation rather than an α-helical conformation like PACAP38 could explain this gain in specificity. Overall, this study has revealed a new function for PACAP38 and related derivatives that can be added to its pleiotropic biological activities. This innovative study could therefore pave the way toward the development of new therapeutic agents against multiresistant bacteria, and more specifically the Burkholderia cenocepacia complex.

Indexed as

AnimalsAnti-Bacterial AgentsBurkholderia cepacia complexCHO CellsCricetulusHumansPituitary Adenylate Cyclase-Activating PolypeptideProtein Structure, SecondaryADCYAP1 protein, humanAnti-Bacterial AgentsPituitary Adenylate Cyclase-Activating Polypeptide

Identifiers

PMID30462698
PMCPMC6248945
OpenAlexW2900577994

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.