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dc.contributor.authorWollein Waldetoft, Kristofer
dc.contributor.authorSvensson, Lisbeth
dc.contributor.authorMörgelin, Matthias
dc.contributor.authorOlin, Anders I
dc.contributor.authorNitsche-Schmitz, D Patric
dc.contributor.authorBjörck, Lars
dc.contributor.authorFrick, Inga-Maria
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.
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
refterms.dateFOA2018-06-13T19:47:23Z
html.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.


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