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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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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 |
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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 |
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