Streptococcal surface proteins activate the contact system and control its antibacterial activity.
Name:
Wollein Waldetoft et al_final.pdf
Size:
2.921Mb
Format:
PDF
Description:
Open Access publication
Average rating
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Authors
Wollein Waldetoft, KristoferSvensson, Lisbeth
Mörgelin, Matthias
Olin, Anders I
Nitsche-Schmitz, D Patric
Björck, Lars
Frick, Inga-Maria
Issue Date
2012-07-20
Metadata
Show full item recordAbstract
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.Citation
Streptococcal surface proteins activate the contact system and control its antibacterial activity. 2012, 287 (30):25010-8 J. Biol. Chem.Affiliation
Division of Infection Medicine, Department of Clinical Sciences, Lund University, SE-221 84 Lund, Sweden. kristofer.wollein_waldetoft@med.lu.sePubMed ID
22648411Type
ArticleLanguage
enISSN
1083-351Xae974a485f413a2113503eed53cd6c53
10.1074/jbc.M112.373217
Scopus Count
The following license files are associated with this item:
Related articles
- The contact system--a novel branch of innate immunity generating antibacterial peptides.
- Authors: Frick IM, Akesson P, Herwald H, Mörgelin M, Malmsten M, Nägler DK, Björck L
- Issue date: 2006 Nov 29
- Interaction of the Human Contact System with Pathogens-An Update.
- Authors: Oehmcke-Hecht S, Köhler J
- Issue date: 2018
- Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q.
- Authors: Nitsche-Schmitz DP, Johansson HM, Sastalla I, Reissmann S, Frick IM, Chhatwal GS
- Issue date: 2007 Jun 15
- Protein FOG is a moderate inducer of MIG/CXCL9, and group G streptococci are more tolerant than group A streptococci to this chemokine's antibacterial effect.
- Authors: Linge HM, Sastalla I, Nitsche-Schmitz DP, Egesten A, Frick IM
- Issue date: 2007 Nov
- Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens.
- Authors: LaRock CN, Nizet V
- Issue date: 2015 Nov