2.50
Hdl Handle:
http://hdl.handle.net/10033/246132
Title:
Streptococcal surface proteins activate the contact system and control its antibacterial activity.
Authors:
Wollein Waldetoft, Kristofer; Svensson, Lisbeth; Mörgelin, Matthias; Olin, Anders I; Nitsche-Schmitz, D Patric; Björck, Lars; Frick, Inga-Maria
Abstract:
Group G streptococci (GGS) are important bacterial pathogens in humans. Here, we investigated the interactions between GGS and the contact system, a procoagulant and proinflammatory proteolytic cascade that, upon activation, also generates antibacterial peptides. Two surface proteins of GGS, protein FOG and protein G (PG), were found to bind contact system proteins. Experiments utilizing contact protein-deficient human plasma and isogenic GGS mutant strains lacking FOG or PG showed that FOG and PG both activate the procoagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen, generating the proinflammatory bradykinin peptide and additional high molecular weight kininogen fragments containing the antimicrobial peptide NAT-26. On the other hand, PG protected the bacteria against the antibacterial effect of NAT-26. These findings underline the significance of the contact system in innate immunity and demonstrate that GGS have evolved surface proteins to exploit and modulate its effects.
Affiliation:
Division of Infection Medicine, Department of Clinical Sciences, Lund University, SE-221 84 Lund, Sweden. kristofer.wollein_waldetoft@med.lu.se
Citation:
Streptococcal surface proteins activate the contact system and control its antibacterial activity. 2012, 287 (30):25010-8 J. Biol. Chem.
Journal:
The Journal of biological chemistry
Issue Date:
20-Jul-2012
URI:
http://hdl.handle.net/10033/246132
DOI:
10.1074/jbc.M112.373217
PubMed ID:
22648411
Type:
Article
Language:
en
ISSN:
1083-351X
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorWollein Waldetoft, Kristoferen_GB
dc.contributor.authorSvensson, Lisbethen_GB
dc.contributor.authorMörgelin, Matthiasen_GB
dc.contributor.authorOlin, Anders Ien_GB
dc.contributor.authorNitsche-Schmitz, D Patricen_GB
dc.contributor.authorBjörck, Larsen_GB
dc.contributor.authorFrick, Inga-Mariaen_GB
dc.date.accessioned2012-09-27T09:54:17Z-
dc.date.available2012-09-27T09:54:17Z-
dc.date.issued2012-07-20-
dc.identifier.citationStreptococcal surface proteins activate the contact system and control its antibacterial activity. 2012, 287 (30):25010-8 J. Biol. Chem.en_GB
dc.identifier.issn1083-351X-
dc.identifier.pmid22648411-
dc.identifier.doi10.1074/jbc.M112.373217-
dc.identifier.urihttp://hdl.handle.net/10033/246132-
dc.description.abstractGroup G streptococci (GGS) are important bacterial pathogens in humans. Here, we investigated the interactions between GGS and the contact system, a procoagulant and proinflammatory proteolytic cascade that, upon activation, also generates antibacterial peptides. Two surface proteins of GGS, protein FOG and protein G (PG), were found to bind contact system proteins. Experiments utilizing contact protein-deficient human plasma and isogenic GGS mutant strains lacking FOG or PG showed that FOG and PG both activate the procoagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen, generating the proinflammatory bradykinin peptide and additional high molecular weight kininogen fragments containing the antimicrobial peptide NAT-26. On the other hand, PG protected the bacteria against the antibacterial effect of NAT-26. These findings underline the significance of the contact system in innate immunity and demonstrate that GGS have evolved surface proteins to exploit and modulate its effects.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to The Journal of biological chemistryen_GB
dc.titleStreptococcal surface proteins activate the contact system and control its antibacterial activity.en
dc.typeArticleen
dc.contributor.departmentDivision of Infection Medicine, Department of Clinical Sciences, Lund University, SE-221 84 Lund, Sweden. kristofer.wollein_waldetoft@med.lu.seen_GB
dc.identifier.journalThe Journal of biological chemistryen_GB

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.