Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2220315
- author
- 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
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 287
- issue
- 2
- pages
- 1415 - 1425
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000299170300055
- pmid:22117078
- scopus:84855510493
- pmid:22117078
- 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
- 2016-04-01 10:30:46
- date last changed
- 2023-01-02 05:20:52
@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 = {{American Society for Biochemistry and Molecular Biology}}, 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}}, doi = {{10.1074/jbc.M111.267674}}, volume = {{287}}, year = {{2012}}, }