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Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes.

Frick, Inga-Maria LU ; Shannon, Oonagh LU ; Åkesson, Per LU ; Mörgelin, Matthias LU ; Collin, Mattias LU ; Schmidtchen, Artur LU and Björck, Lars LU (2011) In Journal of Biological Chemistry 286. p.1331-1340
Abstract
Recent studies have shown that activation of the complement and contact systems results in the generation of antibacterial peptides. Streptococcus pyogenes, a major bacterial pathogen in humans, exists in more than one hundred different serotypes due to sequence variation in the surface-associated M protein. Cases of invasive and life-threatening S. pyogenes infections are commonly associated with isolates of the M1 serotype, and in contrast to the large majority of M serotypes, M1 isolates all secrete the SIC protein. Here we show that SIC interferes with the activation of the contact system, and blocks the activity of antibacterial peptides generated through complement and contact activation. This effect promotes the growth of S.... (More)
Recent studies have shown that activation of the complement and contact systems results in the generation of antibacterial peptides. Streptococcus pyogenes, a major bacterial pathogen in humans, exists in more than one hundred different serotypes due to sequence variation in the surface-associated M protein. Cases of invasive and life-threatening S. pyogenes infections are commonly associated with isolates of the M1 serotype, and in contrast to the large majority of M serotypes, M1 isolates all secrete the SIC protein. Here we show that SIC interferes with the activation of the contact system, and blocks the activity of antibacterial peptides generated through complement and contact activation. This effect promotes the growth of S. pyogenes in human plasma, and in a mouse model of S. pyogenes sepsis, SIC enhances bacterial dissemination, results which help to explain the high frequency of severe S. pyogenes infections caused by isolates of the M1 serotype. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
286
pages
1331 - 1340
publisher
ASBMB
external identifiers
  • wos:000286005000045
  • pmid:21068386
  • scopus:78651407006
ISSN
1083-351X
DOI
10.1074/jbc.M110.178350
language
English
LU publication?
yes
id
b3b4b22f-ae23-49ee-8693-86bb5b236152 (old id 1732084)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21068386?dopt=Abstract
date added to LUP
2010-12-01 11:47:51
date last changed
2017-09-10 03:24:50
@article{b3b4b22f-ae23-49ee-8693-86bb5b236152,
  abstract     = {Recent studies have shown that activation of the complement and contact systems results in the generation of antibacterial peptides. Streptococcus pyogenes, a major bacterial pathogen in humans, exists in more than one hundred different serotypes due to sequence variation in the surface-associated M protein. Cases of invasive and life-threatening S. pyogenes infections are commonly associated with isolates of the M1 serotype, and in contrast to the large majority of M serotypes, M1 isolates all secrete the SIC protein. Here we show that SIC interferes with the activation of the contact system, and blocks the activity of antibacterial peptides generated through complement and contact activation. This effect promotes the growth of S. pyogenes in human plasma, and in a mouse model of S. pyogenes sepsis, SIC enhances bacterial dissemination, results which help to explain the high frequency of severe S. pyogenes infections caused by isolates of the M1 serotype.},
  author       = {Frick, Inga-Maria and Shannon, Oonagh and Åkesson, Per and Mörgelin, Matthias and Collin, Mattias and Schmidtchen, Artur and Björck, Lars},
  issn         = {1083-351X},
  language     = {eng},
  pages        = {1331--1340},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes.},
  url          = {http://dx.doi.org/10.1074/jbc.M110.178350},
  volume       = {286},
  year         = {2011},
}