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

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Author

Summary, in English

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.

Publishing year

2012

Language

English

Pages

1415-1425

Publication/Series

Journal of Biological Chemistry

Volume

287

Issue

2

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Infectious Medicine

Status

Published

Research group

  • Quantitative infection biology
  • Infection Medicine Proteomics
  • epIgG

ISBN/ISSN/Other

  • ISSN: 1083-351X