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Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics.

Malmström, Johan LU ; Karlsson, Christofer LU ; Nordenfelt, Pontus LU ; Ossola, Reto; Weisser, Hendrik; Quandt, Andreas; Hansson, Karin; Aebersold, Ruedi; Malmstrom, Lars and Björck, Lars LU (2012) In Journal of Biological Chemistry 287(2). p.1415-1425
Abstract
Streptococcus pyogenes is a major bacterial pathogen and a potent inducer of inflammation causing plasma leakage at the site of infection. A combination of label free quantitative mass spectrometry-based proteomics strategies were used to measure how the intracellular proteome homeostasis of S. pyogenes is influenced by the presence of human plasma, identifying and quantifying 842 proteins. In plasma the bacterium modifies its production of 213 proteins, and the most pronounced change was the complete down-regulation of proteins required for fatty acid biosynthesis (FAB). Fatty acids are transported by albumin (HSA) in plasma. S. pyogenes expresses HSA-binding surface proteins, and HSA carrying fatty acids reduced the amount of FAB... (More)
Streptococcus pyogenes is a major bacterial pathogen and a potent inducer of inflammation causing plasma leakage at the site of infection. A combination of label free quantitative mass spectrometry-based proteomics strategies were used to measure how the intracellular proteome homeostasis of S. pyogenes is influenced by the presence of human plasma, identifying and quantifying 842 proteins. In plasma the bacterium modifies its production of 213 proteins, and the most pronounced change was the complete down-regulation of proteins required for fatty acid biosynthesis (FAB). Fatty acids are transported by albumin (HSA) in plasma. S. pyogenes expresses HSA-binding surface proteins, and HSA carrying fatty acids reduced the amount of FAB proteins to the same extent as plasma. The results clarify the function of HSA-binding proteins in S. pyogenes and underline the power of the quantitative mass spectrometry strategy used here to investigate bacterial adaptation to a given environment. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
287
issue
2
pages
1415 - 1425
publisher
ASBMB
external identifiers
  • wos:000299170300055
  • pmid:22117078
  • scopus:84855510493
ISSN
1083-351X
DOI
10.1074/jbc.M111.267674
language
English
LU publication?
yes
id
c57f19fb-4660-4aac-8398-cdf2cee63091 (old id 2220315)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/22117078?dopt=Abstract
date added to LUP
2011-12-03 10:20:39
date last changed
2017-10-22 03:16:57
@article{c57f19fb-4660-4aac-8398-cdf2cee63091,
  abstract     = {Streptococcus pyogenes is a major bacterial pathogen and a potent inducer of inflammation causing plasma leakage at the site of infection. A combination of label free quantitative mass spectrometry-based proteomics strategies were used to measure how the intracellular proteome homeostasis of S. pyogenes is influenced by the presence of human plasma, identifying and quantifying 842 proteins. In plasma the bacterium modifies its production of 213 proteins, and the most pronounced change was the complete down-regulation of proteins required for fatty acid biosynthesis (FAB). Fatty acids are transported by albumin (HSA) in plasma. S. pyogenes expresses HSA-binding surface proteins, and HSA carrying fatty acids reduced the amount of FAB proteins to the same extent as plasma. The results clarify the function of HSA-binding proteins in S. pyogenes and underline the power of the quantitative mass spectrometry strategy used here to investigate bacterial adaptation to a given environment.},
  author       = {Malmström, Johan and Karlsson, Christofer and Nordenfelt, Pontus and Ossola, Reto and Weisser, Hendrik and Quandt, Andreas and Hansson, Karin and Aebersold, Ruedi and Malmstrom, Lars and Björck, Lars},
  issn         = {1083-351X},
  language     = {eng},
  number       = {2},
  pages        = {1415--1425},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics.},
  url          = {http://dx.doi.org/10.1074/jbc.M111.267674},
  volume       = {287},
  year         = {2012},
}