Streptococcal surface proteins activate the contact system and control its antibacterial activity.
Wollein Waldetoft et al_final.pdf
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AuthorsWollein Waldetoft, Kristofer
Olin, Anders I
Nitsche-Schmitz, D Patric
MetadataShow full item record
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.
CitationStreptococcal surface proteins activate the contact system and control its antibacterial activity. 2012, 287 (30):25010-8 J. Biol. Chem.
AffiliationDivision of Infection Medicine, Department of Clinical Sciences, Lund University, SE-221 84 Lund, Sweden. email@example.com
The following license files are associated with this item:
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