Streptococcal surface proteins activate the contact system and control its antibacterial activity.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2859957
- author
- Wollein Waldetoft, Kristofer LU ; Svensson, Lisbeth LU ; Mörgelin, Matthias LU ; Olin, Anders LU ; Nitsche, Patric ; Björck, Lars LU and Frick, Inga-Maria LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 287
- issue
- 30
- pages
- 25010 - 25018
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000306651700014
- pmid:22648411
- scopus:84864085487
- pmid:22648411
- 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
- 2016-04-01 10:38:21
- date last changed
- 2022-01-26 01:07:40
@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 = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Streptococcal surface proteins activate the contact system and control its antibacterial activity.}}, url = {{https://lup.lub.lu.se/search/files/2015744/3053747.pdf}}, doi = {{10.1074/jbc.M112.373217}}, volume = {{287}}, year = {{2012}}, }