Catestatin in innate immunity and Cateslytin-derived peptides against superbugs

Abstract Chromogranin A (CgA) is the precursor of several antimicrobial peptides, such as Catestatin (Cts, bovine CgA344-364), initially described as a potent inhibitor of catecholamines. This peptide displays direct antimicrobial activities and contributes to immune system regulation. The aim of th...

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Autores principales:	Francesco Scavello, Angela Mutschler, Sophie Hellé, Francis Schneider, Sylvette Chasserot-Golaz, Jean-Marc Strub, Sarah Cianferani, Youssef Haikel, Marie-Hélène Metz-Boutigue
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/902cf7b567b743c0ab768f0daa34fe84
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spelling	oai:doaj.org-article:902cf7b567b743c0ab768f0daa34fe842021-12-02T18:49:16ZCatestatin in innate immunity and Cateslytin-derived peptides against superbugs10.1038/s41598-021-94749-62045-2322https://doaj.org/article/902cf7b567b743c0ab768f0daa34fe842021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-94749-6https://doaj.org/toc/2045-2322Abstract Chromogranin A (CgA) is the precursor of several antimicrobial peptides, such as Catestatin (Cts, bovine CgA344-364), initially described as a potent inhibitor of catecholamines. This peptide displays direct antimicrobial activities and contributes to immune system regulation. The aim of the present study is to investigate a designed peptide based on Cts to fight infections against superbugs and more particularly Staphylococcus aureus. In addition to Cateslytin (Ctl, bovine CgA344-358), the active domain of Catestatin, several peptides including dimers, D-isomer and the new designed peptide DOPA-K-DOPA-K-DOPA-TLRGGE-RSMRLSFRARGYGFR (Dopa5T-Ctl) were prepared and tested. Cateslytin is resistant to bacterial degradation and does not induce bacterial resistance. The interaction of Catestatin with immune dermal cells (dendritic cells DC1a, dermal macrophages CD14 and macrophages) was analyzed by using confocal microscopy and cytokine release assay. The dimers and D-isomer of Ctl were tested against a large variety of bacteria showing the potent antibacterial activity of the D-isomer. The peptide Dopa5T-Ctl is able to induce the self-killing of S. aureus after release of Ctl by the endoprotease Glu-C produced by this pathogen. It permits localized on-demand delivery of the antimicrobial drug directly at the infectious site.Francesco ScavelloAngela MutschlerSophie HelléFrancis SchneiderSylvette Chasserot-GolazJean-Marc StrubSarah CianferaniYoussef HaikelMarie-Hélène Metz-BoutigueNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Francesco Scavello Angela Mutschler Sophie Hellé Francis Schneider Sylvette Chasserot-Golaz Jean-Marc Strub Sarah Cianferani Youssef Haikel Marie-Hélène Metz-Boutigue Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
description	Abstract Chromogranin A (CgA) is the precursor of several antimicrobial peptides, such as Catestatin (Cts, bovine CgA344-364), initially described as a potent inhibitor of catecholamines. This peptide displays direct antimicrobial activities and contributes to immune system regulation. The aim of the present study is to investigate a designed peptide based on Cts to fight infections against superbugs and more particularly Staphylococcus aureus. In addition to Cateslytin (Ctl, bovine CgA344-358), the active domain of Catestatin, several peptides including dimers, D-isomer and the new designed peptide DOPA-K-DOPA-K-DOPA-TLRGGE-RSMRLSFRARGYGFR (Dopa5T-Ctl) were prepared and tested. Cateslytin is resistant to bacterial degradation and does not induce bacterial resistance. The interaction of Catestatin with immune dermal cells (dendritic cells DC1a, dermal macrophages CD14 and macrophages) was analyzed by using confocal microscopy and cytokine release assay. The dimers and D-isomer of Ctl were tested against a large variety of bacteria showing the potent antibacterial activity of the D-isomer. The peptide Dopa5T-Ctl is able to induce the self-killing of S. aureus after release of Ctl by the endoprotease Glu-C produced by this pathogen. It permits localized on-demand delivery of the antimicrobial drug directly at the infectious site.
format	article
author	Francesco Scavello Angela Mutschler Sophie Hellé Francis Schneider Sylvette Chasserot-Golaz Jean-Marc Strub Sarah Cianferani Youssef Haikel Marie-Hélène Metz-Boutigue
author_facet	Francesco Scavello Angela Mutschler Sophie Hellé Francis Schneider Sylvette Chasserot-Golaz Jean-Marc Strub Sarah Cianferani Youssef Haikel Marie-Hélène Metz-Boutigue
author_sort	Francesco Scavello
title	Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
title_short	Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
title_full	Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
title_fullStr	Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
title_full_unstemmed	Catestatin in innate immunity and Cateslytin-derived peptides against superbugs
title_sort	catestatin in innate immunity and cateslytin-derived peptides against superbugs
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/902cf7b567b743c0ab768f0daa34fe84
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Catestatin in innate immunity and Cateslytin-derived peptides against superbugs

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