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

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Bibtex

@article{c57f19fb46604aac8398cdf2cee63091,
title = "Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics.",
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 = "Johan Malmstr{\"o}m and Christofer Karlsson and Pontus Nordenfelt and Reto Ossola and Hendrik Weisser and Andreas Quandt and Karin Hansson and Ruedi Aebersold and Lars Malmstrom and Lars Bj{\"o}rck",
year = "2012",
doi = "10.1074/jbc.M111.267674",
language = "English",
volume = "287",
pages = "1415--1425",
journal = "Journal of Biological Chemistry",
issn = "1083-351X",
publisher = "ASBMB",
number = "2",

}