Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
JOURNAL OF PROTEOME RESEARCH(2010)
摘要
Most of the Staphylococcus aureus virulence factors are either cell surface exposed or secreted. Here we report a global and quantitative analysis of staphylococcal cell surface-associated proteins using a combination of (NN)-N-14-N-15 metabolic labeling, biotinylation, and GeLC-MS/MS. To address the important question of S. aureus pathophysiology, we analyzed the influence of the alternative sigma factor sigma(B) on the expression of cell surface-associated proteins. Therefore, we compared the methicillin-resistant S. aureus wild-type strain COL with its sigB mutant, because sigma(B) might play a crucial role in the pattern of the surface proteome. A total of 296 proteins from growing and nongrowing cells could be quantified. One third of these proteins are known as cell surface-associated, including 3 sortase substrates, 3 cell wall-associated proteins, 35 lipo-, 23 membrane-, and 34 signal peptide-containing proteins comparing wild-type and sigB mutant. Fourty nine surface-associated proteins were modulated by sigma(B), including 21 proteins already known to be SigB-dependent or SigB-influenced. More proteins were down- (31 proteins) than up-regulated (18 proteins) in the sigB mutant. Our approach revealed 28 surface-associated proteins not previously reported as SigB-dependent or -influenced, expanding the group of surface-associated proteins and virulence factors modulated by SigB.
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关键词
biotinylation,cell surface proteins,mass spectrometry,(NN)-N-14-N-15 metabolic labeling,SigmaB,Staphylococcus aureus
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