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Structure, biosynthesis, and biological activity of succinylated forms of bacteriocin BacSp222

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dc.abstract.enBacSp222 is a multifunctional peptide produced by Staphylococcus pseudintermedius 222. This 50-amino acid long peptide belongs to subclass IId of bacteriocins and forms a four-helix bundle molecule. In addition to bactericidal functions, BacSp222 possesses also features of a virulence factor, manifested in immunomodulatory and cytotoxic activities toward eukaryotic cells. In the present study, we demonstrate that BacSp222 is produced in several post-translationally modified forms, succinylated at the "-amino group of lysine residues. Such modifications have not been previously described for any bacteriocins. NMR and circular dichroism spectroscopy studies have shown that the modifications do not alter the spatial structure of the peptide. At the same time, succinylation significantly diminishes its bactericidal and cytotoxic potential. We demonstrate that the modification of the bacteriocin is an effect of non-enzymatic reaction with a highly reactive intracellular metabolite, i.e., succinyl-coenzyme A. The production of succinylated forms of the bacteriocin depends on environmental factors and on the access of bacteria to nutrients. Our study indicates that the production of succinylated forms of bacteriocin occurs in response to the changing environment, protects producer cells against the autotoxicity of the excreted peptide, and limits the pathogenicity of the strain.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorBzowska, Monika
dc.contributor.authorBocheńska, Oliwia
dc.contributor.authorWlizło, Agnieszka
dc.contributor.authorŚmiałek, Justyna
dc.contributor.authorKozik, Andrzej
dc.contributor.authorDubin, Grzegorz
dc.contributor.authorMak, Paweł
dc.contributor.authorNowakowski, Michał
dc.date.accessioned2024-01-26T08:22:04Z
dc.date.available2024-01-26T08:22:04Z
dc.date.copyright2021-06-10
dc.date.issued2021
dc.description.accesstimeAT_PUBLICATION
dc.description.financePublikacja bezkosztowa
dc.description.number12
dc.description.versionFINAL_PUBLISHED
dc.description.volume22
dc.identifier.doi10.3390/IJMS22126256
dc.identifier.issn1422-0067
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/120925
dc.identifier.weblinkhttp://www.scopus.com/inward/record.url?eid=2-s2.0-85107484724&partnerID=MN8TOARS
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.relation.pages6256
dc.rightsCC-BY
dc.sciencecloudnosend
dc.subject.enbacteriocin
dc.subject.encytotoxic
dc.subject.enantibacterial
dc.subject.enStaphylococcus pseudintermedius
dc.subject.ensuccinylation
dc.subject.ensuccinylcoenzyme A
dc.subject.ennuclear magnetic resonance (NMR)
dc.subject.enKrebs/tricarboxylic acids cycle
dc.titleStructure, biosynthesis, and biological activity of succinylated forms of bacteriocin BacSp222
dc.typeJournalArticle
dspace.entity.typePublication