title: Cateslytin, a chromogranin A derived peptide is active against Staphylococcus aureus and resistant to degradation by its proteases.
abstract: 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.
authors.affiliation: Inserm UMR-1121, Université de Strasbourg, Strasbourg, France.
authors.forename: Rizwan
authors.initials: R
authors.lastname: Aslam
authors.forename: Céline
authors.initials: C
authors.lastname: Marban
authors.forename: Christian
authors.initials: C
authors.lastname: Corazzol
authors.forename: François
authors.initials: F
authors.lastname: Jehl
authors.forename: François
authors.initials: F
authors.lastname: Delalande
authors.forename: Alain
authors.initials: A
authors.lastname: Van Dorsselaer
authors.forename: Gilles
authors.initials: G
authors.lastname: Prévost
authors.forename: Youssef
authors.initials: Y
authors.lastname: Haïkel
authors.forename: Corinne
authors.initials: C
authors.lastname: Taddei
authors.forename: Francis
authors.initials: F
authors.lastname: Schneider
authors.forename: Marie-Hélène
authors.initials: MH
authors.lastname: Metz-Boutigue
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D053379:Chromogranin A / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013211:Staphylococcus aureus / Q000187:drug effects* / Q000201:enzymology*
chemical_list: D000890:Anti-Infective Agents; D053379:Chromogranin A; D010455:Peptides; D010447:Peptide Hydrolases
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