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

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Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics. / Malmström, Johan; Karlsson, Christofer; Nordenfelt, Pontus; Ossola, Reto; Weisser, Hendrik; Quandt, Andreas; Hansson, Karin; Aebersold, Ruedi; Malmstrom, Lars; Björck, Lars.

In: Journal of Biological Chemistry, Vol. 287, No. 2, 2012, p. 1415-1425.

Research output: Contribution to journalArticle

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Malmström, Johan ; Karlsson, Christofer ; Nordenfelt, Pontus ; Ossola, Reto ; Weisser, Hendrik ; Quandt, Andreas ; Hansson, Karin ; Aebersold, Ruedi ; Malmstrom, Lars ; Björck, Lars. / Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 2. pp. 1415-1425.

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TY - JOUR

T1 - Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry based proteomics.

AU - Malmström, Johan

AU - Karlsson, Christofer

AU - Nordenfelt, Pontus

AU - Ossola, Reto

AU - Weisser, Hendrik

AU - Quandt, Andreas

AU - Hansson, Karin

AU - Aebersold, Ruedi

AU - Malmstrom, Lars

AU - Björck, Lars

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M111.267674

DO - 10.1074/jbc.M111.267674

M3 - Article

C2 - 22117078

VL - 287

SP - 1415

EP - 1425

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 2

ER -