Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1732084
- author
- Frick, Inga-Maria LU ; Shannon, Oonagh LU ; Åkesson, Per LU ; Mörgelin, Matthias LU ; Collin, Mattias LU ; Schmidtchen, Artur LU and Björck, Lars LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 286
- pages
- 1331 - 1340
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000286005000045
- pmid:21068386
- scopus:78651407006
- pmid:21068386
- 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
- 2016-04-01 10:59:10
- date last changed
- 2022-01-26 04:31:16
@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 = {{American Society for Biochemistry and Molecular Biology}}, 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 = {{https://lup.lub.lu.se/search/files/2285735/1748041.pdf}}, doi = {{10.1074/jbc.M110.178350}}, volume = {{286}}, year = {{2011}}, }