Cargando…

Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases

Innate immunity involving antimicrobial peptides represents an integrated and highly effective system of molecular and cellular mechanisms that protects host against infections. One of the most frequent hospital-acquired pathogens, Staphylococcus aureus, capable of producing proteolytic enzymes, whi...

Descripción completa

Detalles Bibliográficos
Autores principales: Aslam, Rizwan, Marban, Céline, Corazzol, Christian, Jehl, François, Delalande, François, Van Dorsselaer, Alain, Prévost, Gilles, Haïkel, Youssef, Taddei, Corinne, Schneider, Francis, Metz-Boutigue, Marie-Hélène
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3722296/
https://www.ncbi.nlm.nih.gov/pubmed/23894389
http://dx.doi.org/10.1371/journal.pone.0068993
_version_ 1782278176951500800
author Aslam, Rizwan
Marban, Céline
Corazzol, Christian
Jehl, François
Delalande, François
Van Dorsselaer, Alain
Prévost, Gilles
Haïkel, Youssef
Taddei, Corinne
Schneider, Francis
Metz-Boutigue, Marie-Hélène
author_facet Aslam, Rizwan
Marban, Céline
Corazzol, Christian
Jehl, François
Delalande, François
Van Dorsselaer, Alain
Prévost, Gilles
Haïkel, Youssef
Taddei, Corinne
Schneider, Francis
Metz-Boutigue, Marie-Hélène
author_sort Aslam, Rizwan
collection PubMed
description Innate immunity involving antimicrobial peptides represents an integrated and highly effective system of molecular and cellular mechanisms that protects host against infections. One of the most frequent hospital-acquired pathogens, Staphylococcus aureus, capable of producing proteolytic enzymes, which can degrade the host defence agents and tissue components. Numerous antimicrobial peptides derived from chromogranins, are secreted by nervous, endocrine and immune cells during stress conditions. These kill microorganisms by their lytic effect at micromolar range, using a pore-forming mechanism against Gram-positive bacteria, filamentous fungi and yeasts. In this study, we tested antimicrobial activity of chromogranin A-derived peptides (catestatin and cateslytin) against S. aureus and analysed S. aureus-mediated proteolysis of these peptides using HPLC, sequencing and MALDI-TOF mass spectrometry. Interestingly, this study is the first to demonstrate that cateslytin, the active domain of catestatin, is active against S. aureus and is interestingly resistant to degradation by S. aureus proteases.
format Online
Article
Text
id pubmed-3722296
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-37222962013-07-26 Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases Aslam, Rizwan Marban, Céline Corazzol, Christian Jehl, François Delalande, François Van Dorsselaer, Alain Prévost, Gilles Haïkel, Youssef Taddei, Corinne Schneider, Francis Metz-Boutigue, Marie-Hélène PLoS One Research Article Innate immunity involving antimicrobial peptides represents an integrated and highly effective system of molecular and cellular mechanisms that protects host against infections. One of the most frequent hospital-acquired pathogens, Staphylococcus aureus, capable of producing proteolytic enzymes, which can degrade the host defence agents and tissue components. Numerous antimicrobial peptides derived from chromogranins, are secreted by nervous, endocrine and immune cells during stress conditions. These kill microorganisms by their lytic effect at micromolar range, using a pore-forming mechanism against Gram-positive bacteria, filamentous fungi and yeasts. In this study, we tested antimicrobial activity of chromogranin A-derived peptides (catestatin and cateslytin) against S. aureus and analysed S. aureus-mediated proteolysis of these peptides using HPLC, sequencing and MALDI-TOF mass spectrometry. Interestingly, this study is the first to demonstrate that cateslytin, the active domain of catestatin, is active against S. aureus and is interestingly resistant to degradation by S. aureus proteases. Public Library of Science 2013-07-24 /pmc/articles/PMC3722296/ /pubmed/23894389 http://dx.doi.org/10.1371/journal.pone.0068993 Text en © 2013 Aslam et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Aslam, Rizwan
Marban, Céline
Corazzol, Christian
Jehl, François
Delalande, François
Van Dorsselaer, Alain
Prévost, Gilles
Haïkel, Youssef
Taddei, Corinne
Schneider, Francis
Metz-Boutigue, Marie-Hélène
Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title_full Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title_fullStr Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title_full_unstemmed Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title_short Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases
title_sort cateslytin, a chromogranin a derived peptide is active against staphylococcus aureus and resistant to degradation by its proteases
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3722296/
https://www.ncbi.nlm.nih.gov/pubmed/23894389
http://dx.doi.org/10.1371/journal.pone.0068993
work_keys_str_mv AT aslamrizwan cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT marbanceline cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT corazzolchristian cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT jehlfrancois cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT delalandefrancois cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT vandorsselaeralain cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT prevostgilles cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT haikelyoussef cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT taddeicorinne cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT schneiderfrancis cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases
AT metzboutiguemariehelene cateslytinachromograninaderivedpeptideisactiveagainststaphylococcusaureusandresistanttodegradationbyitsproteases