Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans

2015
journal article
article
21
dc.abstract.enBackground. Candida albicans yeast produces 10 distinct secreted aspartic proteases (Saps), which are some of the most important virulence factors of this pathogenic fungus. One of the suggested roles of Saps is their deregulating effect on various proteolytic cascades that constitute the major homeostatic systems in human hosts, including blood coagulation, fibrinolysis, and kallikrein-kinin systems. This study compared the characteristics of the action of all 10 Saps on human kininogens, which results in generating proinflammatory bradykinin-related peptides (kinins). Results. Recombinant forms of Saps, heterologously overexpressed in Pichia pastoris were applied. Except for Sap7 and Sap10, all Saps effectively cleaved the kininogens, with the highest hydrolytic activity toward the low-molecular-mass form (LK). Sap1–6 and 8 produced a biologically active kinin-Met-Lys-bradykinin-and Sap3 was exceptional in terms of the kinin-releasing yield (>60% LK at pH 5.0 after 24 hours). Des-Arg^1-bradykinin was released from LK by Sap9 at a comparably high yield, but this peptide was assumed to be biologically inactive because it was unable to interact with cellular B2-type kinin receptors. However, the collaborative actions of Sap9 and Sap1, −2, −4–6, and −8 on LK rerouted kininogen cleavage toward the high-yield release of the biologically active Met-Lys-bradykinin. Conclusions. Our present results, together with the available data on the expression of individual SAP genes in candidal infection models, suggest a biological potential of Saps to produce kinins at the infection foci. The kinin release during candidiasis can involve predominant and complementary contributions of two different Sap3- and Sap9-dependent mechanisms.pl
dc.affiliationWydział Biochemii, Biofizyki i Biotechnologii : Zakład Biochemii Analitycznejpl
dc.contributor.authorKozik, Andrzej - 129351 pl
dc.contributor.authorGogól, Mariusz - 118240 pl
dc.contributor.authorBocheńska, Oliwia - 173990 pl
dc.contributor.authorKarkowska-Kuleta, Justyna - 104458 pl
dc.contributor.authorWolak, Natalia - 109386 pl
dc.contributor.authorKamysz, Wojciechpl
dc.contributor.authorAoki, Watarupl
dc.contributor.authorUeda, Mitsuyoshipl
dc.contributor.authorFaussner, Alexanderpl
dc.contributor.authorRąpała-Kozik, Maria - 131641 pl
dc.date.accessioned2015-05-21T09:25:57Z
dc.date.available2015-05-21T09:25:57Z
dc.date.issued2015pl
dc.date.openaccess0
dc.description.accesstimew momencie opublikowania
dc.description.versionostateczna wersja wydawcy
dc.description.volume15pl
dc.identifier.articleid60pl
dc.identifier.doi10.1186/s12866-015-0394-8pl
dc.identifier.eissn1471-2180pl
dc.identifier.projectROD UJ / Ppl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/7666
dc.languageengpl
dc.language.containerengpl
dc.rightsUdzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa*
dc.rights.licenceCC-BY
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcode.pl*
dc.share.typeotwarte czasopismo
dc.subject.encandidiasispl
dc.subject.enhuman kininogenpl
dc.subject.enMet-Lys-bradykininpl
dc.subject.endes-Arg-kininspl
dc.subject.enbradykinin B2-subtype receptorspl
dc.subject.enPichia pastorispl
dc.subtypeArticlepl
dc.titleKinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicanspl
dc.title.journalBMC Microbiologypl
dc.title.volumeMarchpl
dc.typeJournalArticlepl
dspace.entity.typePublication
dc.abstract.enpl
Background. Candida albicans yeast produces 10 distinct secreted aspartic proteases (Saps), which are some of the most important virulence factors of this pathogenic fungus. One of the suggested roles of Saps is their deregulating effect on various proteolytic cascades that constitute the major homeostatic systems in human hosts, including blood coagulation, fibrinolysis, and kallikrein-kinin systems. This study compared the characteristics of the action of all 10 Saps on human kininogens, which results in generating proinflammatory bradykinin-related peptides (kinins). Results. Recombinant forms of Saps, heterologously overexpressed in Pichia pastoris were applied. Except for Sap7 and Sap10, all Saps effectively cleaved the kininogens, with the highest hydrolytic activity toward the low-molecular-mass form (LK). Sap1–6 and 8 produced a biologically active kinin-Met-Lys-bradykinin-and Sap3 was exceptional in terms of the kinin-releasing yield (>60% LK at pH 5.0 after 24 hours). Des-Arg^1-bradykinin was released from LK by Sap9 at a comparably high yield, but this peptide was assumed to be biologically inactive because it was unable to interact with cellular B2-type kinin receptors. However, the collaborative actions of Sap9 and Sap1, −2, −4–6, and −8 on LK rerouted kininogen cleavage toward the high-yield release of the biologically active Met-Lys-bradykinin. Conclusions. Our present results, together with the available data on the expression of individual SAP genes in candidal infection models, suggest a biological potential of Saps to produce kinins at the infection foci. The kinin release during candidiasis can involve predominant and complementary contributions of two different Sap3- and Sap9-dependent mechanisms.
dc.affiliationpl
Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Biochemii Analitycznej
dc.contributor.authorpl
Kozik, Andrzej - 129351
dc.contributor.authorpl
Gogól, Mariusz - 118240
dc.contributor.authorpl
Bocheńska, Oliwia - 173990
dc.contributor.authorpl
Karkowska-Kuleta, Justyna - 104458
dc.contributor.authorpl
Wolak, Natalia - 109386
dc.contributor.authorpl
Kamysz, Wojciech
dc.contributor.authorpl
Aoki, Wataru
dc.contributor.authorpl
Ueda, Mitsuyoshi
dc.contributor.authorpl
Faussner, Alexander
dc.contributor.authorpl
Rąpała-Kozik, Maria - 131641
dc.date.accessioned
2015-05-21T09:25:57Z
dc.date.available
2015-05-21T09:25:57Z
dc.date.issuedpl
2015
dc.date.openaccess
0
dc.description.accesstime
w momencie opublikowania
dc.description.version
ostateczna wersja wydawcy
dc.description.volumepl
15
dc.identifier.articleidpl
60
dc.identifier.doipl
10.1186/s12866-015-0394-8
dc.identifier.eissnpl
1471-2180
dc.identifier.projectpl
ROD UJ / P
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/7666
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa
dc.rights.licence
CC-BY
dc.rights.uri*
http://creativecommons.org/licenses/by/4.0/legalcode.pl
dc.share.type
otwarte czasopismo
dc.subject.enpl
candidiasis
dc.subject.enpl
human kininogen
dc.subject.enpl
Met-Lys-bradykinin
dc.subject.enpl
des-Arg-kinins
dc.subject.enpl
bradykinin B2-subtype receptors
dc.subject.enpl
Pichia pastoris
dc.subtypepl
Article
dc.titlepl
Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans
dc.title.journalpl
BMC Microbiology
dc.title.volumepl
March
dc.typepl
JournalArticle
dspace.entity.type
Publication

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