Evidence map›Paper›PMID 31541146›Full record

ArticleScientific reports2019

Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes.

Elisa Chaparro-Aguirre, Paula J Segura-Ramírez, Flavio L Alves, Karin A Riske, Antonio Miranda, Pedro I Silva Júnior

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Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

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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

6 authors.

Elisa Chaparro-AguirreSpecial Laboratory for Applied Toxinology (LETA), Butantan Institute, São Paulo, 05503-900, Brazil.
Paula J Segura-RamírezSpecial Laboratory for Applied Toxinology (LETA), Butantan Institute, São Paulo, 05503-900, Brazil. paulasegura64@gmail.com.
Flavio L AlvesDepartment of Biophysics, Federal University of São Paulo, São Paulo, 04044-020, Brazil.ORCID http://orcid.org/0000-0002-3874-4473
Karin A RiskeDepartment of Biophysics, Federal University of São Paulo, São Paulo, 04044-020, Brazil.
Antonio MirandaDepartment of Biophysics, Federal University of São Paulo, São Paulo, 04044-020, Brazil.ORCID http://orcid.org/0000-0002-6680-3696
Pedro I Silva JúniorSpecial Laboratory for Applied Toxinology (LETA), Butantan Institute, São Paulo, 05503-900, Brazil.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the most important cellular events in arthropods is the moulting of the cuticle (ecdysis). This process allows them to grow until they reach sexual maturity. Nevertheless, during this stage, the animals are highly exposed to pathogens. Consequently, it can be assumed that arthropods counter with an efficient anti-infective strategy that facilitates their survival during ecdysis. Herein, we characterized a novel antimicrobial peptide called Pinipesin, present in the exuviae extract of the centipede Scolopendra subspinipes subspinipes. The antimicrobial activity of Pinipesin was tested. The haemolytic activity of the peptide was evaluated and its possible mechanism of action was investigated. Identification was carried out by mass spectrometry analysis. Pinipesin displayed potent antimicrobial effects against different microorganisms and showed low haemolytic effects against human erythrocytes at high concentrations. It has a monoisotopic mass of 1213.57 Da, its sequence exhibited high similarity with some cuticular proteins, and it might act intracellularly by interfering with protein synthesis. Our data suggest that Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes. Therefore, it is a promising candidate for the development of non-conventional antibiotics that could help fight infectious diseases and represents an exciting discovery for this taxon.

Indexed as

AnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesArthropod ProteinsArthropodsBacteriaCells, CulturedCircular DichroismErythrocytesFungiHemolysisHumansMicrobial Sensitivity TestsMolecular WeightMoltingAnti-Infective AgentsAntimicrobial Cationic PeptidesArthropod Proteins

Identifiers

PMID31541146
PMCPMC6754450

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Registered trials

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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.