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Streptococcal surface proteins activate the contact system and control its antibacterial activity.

Wollein Waldetoft, Kristofer LU ; Svensson, Lisbeth LU ; Mörgelin, Matthias LU ; Olin, Anders LU ; Nitsche, Patric; Björck, Lars LU and Frick, Inga-Maria LU (2012) In Journal of Biological Chemistry 287(30). p.25010-25018
Abstract
Group G streptococci (GGS) are important bacterial pathogens in humans. Here we investigate the interactions between GGS and the contact system, a pro-coagulant and pro-inflammatory proteolytic cascade, which 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 pro-coagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen (HK), generating the pro-inflammatory bradykinin peptide and additional HK fragments containing the... (More)
Group G streptococci (GGS) are important bacterial pathogens in humans. Here we investigate the interactions between GGS and the contact system, a pro-coagulant and pro-inflammatory proteolytic cascade, which 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 pro-coagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen (HK), generating the pro-inflammatory bradykinin peptide and additional HK fragments containing the antimicrobial peptide NAT-26. PG, on the other hand, 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. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
287
issue
30
pages
25010 - 25018
publisher
ASBMB
external identifiers
  • wos:000306651700014
  • pmid:22648411
  • scopus:84864085487
ISSN
1083-351X
DOI
10.1074/jbc.M112.373217
language
English
LU publication?
yes
id
585e9af3-0b3b-410f-936d-e97c172717bf (old id 2859957)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/22648411?dopt=Abstract
date added to LUP
2012-07-04 11:25:27
date last changed
2017-10-01 03:20:11
@article{585e9af3-0b3b-410f-936d-e97c172717bf,
  abstract     = {Group G streptococci (GGS) are important bacterial pathogens in humans. Here we investigate the interactions between GGS and the contact system, a pro-coagulant and pro-inflammatory proteolytic cascade, which 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 pro-coagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen (HK), generating the pro-inflammatory bradykinin peptide and additional HK fragments containing the antimicrobial peptide NAT-26. PG, on the other hand, 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.},
  author       = {Wollein Waldetoft, Kristofer and Svensson, Lisbeth and Mörgelin, Matthias and Olin, Anders and Nitsche, Patric and Björck, Lars and Frick, Inga-Maria},
  issn         = {1083-351X},
  language     = {eng},
  number       = {30},
  pages        = {25010--25018},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Streptococcal surface proteins activate the contact system and control its antibacterial activity.},
  url          = {http://dx.doi.org/10.1074/jbc.M112.373217},
  volume       = {287},
  year         = {2012},
}