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Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori

Helicobacter pylori is a Gram negative bacterium most frequently associated with human gastrointestinal infections worldwide. The increasing occurrence of antibiotic-resistant isolates of H. pylori constitutes a challenge. The eradication of the microorganism is currently being considered a “high pr...

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Autores principales: Salinas Ibáñez, Ángel Gabriel, Origone, Anabella L., Liggieri, Constanza S., Barberis, Sonia E., Vega, Alba E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9433900/
https://www.ncbi.nlm.nih.gov/pubmed/36060760
http://dx.doi.org/10.3389/fmicb.2022.961958
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author Salinas Ibáñez, Ángel Gabriel
Origone, Anabella L.
Liggieri, Constanza S.
Barberis, Sonia E.
Vega, Alba E.
author_facet Salinas Ibáñez, Ángel Gabriel
Origone, Anabella L.
Liggieri, Constanza S.
Barberis, Sonia E.
Vega, Alba E.
author_sort Salinas Ibáñez, Ángel Gabriel
collection PubMed
description Helicobacter pylori is a Gram negative bacterium most frequently associated with human gastrointestinal infections worldwide. The increasing occurrence of antibiotic-resistant isolates of H. pylori constitutes a challenge. The eradication of the microorganism is currently being considered a “high priority” by the World Health Organization (WHO). In this context, bioactive compounds found in natural products seem to be an effective therapeutic option to develop new antibiotics against the pathogen. In this study, we investigated the effect of asclepain cI, the main purified proteolytic enzyme of the latex of petioles and stems from Asclepia curassavica L. (Asclepiadaceae), a South American native plant, against H. pylori; in order to obtain a natural therapeutic adjuvant and a safe nutraceutical product. Asclepain cI showed antibacterial activity against reference strains and drug-resistant clinical isolates of H. pylori in vitro. A range of minimal inhibitory concentration (MIC) from 1 to 2 μg/ml and minimal bactericidal concentration (MBC) from 2 to 4 μg/ml was obtained, respectively. The action of asclepain cI on the transcription of omp18, ureA, flaA genes showed a significantly decreased expression of the selected pathogenic factors. Furthermore, asclepain cI did not induce toxic effects at the concentrations assayed. Asclepain cI could be considered a highly feasible option to be used as a natural therapeutic adjuvant and a safe nutraceutical product against H. pylori.
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spelling pubmed-94339002022-09-02 Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori Salinas Ibáñez, Ángel Gabriel Origone, Anabella L. Liggieri, Constanza S. Barberis, Sonia E. Vega, Alba E. Front Microbiol Microbiology Helicobacter pylori is a Gram negative bacterium most frequently associated with human gastrointestinal infections worldwide. The increasing occurrence of antibiotic-resistant isolates of H. pylori constitutes a challenge. The eradication of the microorganism is currently being considered a “high priority” by the World Health Organization (WHO). In this context, bioactive compounds found in natural products seem to be an effective therapeutic option to develop new antibiotics against the pathogen. In this study, we investigated the effect of asclepain cI, the main purified proteolytic enzyme of the latex of petioles and stems from Asclepia curassavica L. (Asclepiadaceae), a South American native plant, against H. pylori; in order to obtain a natural therapeutic adjuvant and a safe nutraceutical product. Asclepain cI showed antibacterial activity against reference strains and drug-resistant clinical isolates of H. pylori in vitro. A range of minimal inhibitory concentration (MIC) from 1 to 2 μg/ml and minimal bactericidal concentration (MBC) from 2 to 4 μg/ml was obtained, respectively. The action of asclepain cI on the transcription of omp18, ureA, flaA genes showed a significantly decreased expression of the selected pathogenic factors. Furthermore, asclepain cI did not induce toxic effects at the concentrations assayed. Asclepain cI could be considered a highly feasible option to be used as a natural therapeutic adjuvant and a safe nutraceutical product against H. pylori. Frontiers Media S.A. 2022-08-18 /pmc/articles/PMC9433900/ /pubmed/36060760 http://dx.doi.org/10.3389/fmicb.2022.961958 Text en Copyright © 2022 Salinas Ibáñez, Origone, Liggieri, Barberis and Vega. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Salinas Ibáñez, Ángel Gabriel
Origone, Anabella L.
Liggieri, Constanza S.
Barberis, Sonia E.
Vega, Alba E.
Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title_full Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title_fullStr Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title_full_unstemmed Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title_short Asclepain cI, a proteolytic enzyme from Asclepias curassavica L., a south American plant, against Helicobacter pylori
title_sort asclepain ci, a proteolytic enzyme from asclepias curassavica l., a south american plant, against helicobacter pylori
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9433900/
https://www.ncbi.nlm.nih.gov/pubmed/36060760
http://dx.doi.org/10.3389/fmicb.2022.961958
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