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Surface proteome adaption of Staphylococcus aureus HG001 during biofilm formation

ABSTRACT: We applied an optimized biotinylation approach for quantitative GeLC-MS based analysis of the staphylococcal cell-surface proteome and analyzed the cytoplasmic protein fraction as well in order to elucidate proteomic differences between colony biofilms and planktonic cells.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Martin Moche

LAB HEAD: Dörte Becher

PROVIDER: PXD001395 | Pride | 2015-11-13

REPOSITORIES: Pride

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			Action	DRS
	120520_O1_U3_MM_MA_01.RAW	Raw
	120520_O1_U3_MM_MA_02.RAW	Raw
	120520_O1_U3_MM_MA_03.RAW	Raw
	120520_O1_U3_MM_MA_04.RAW	Raw
	120520_O1_U3_MM_MA_05.RAW	Raw

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Publications

Time-Resolved Analysis of Cytosolic and Surface-Associated Proteins of Staphylococcus aureus HG001 under Planktonic and Biofilm Conditions.

Moche Martin M Schlüter Rabea R Bernhardt Jörg J Plate Kristina K Riedel Katharina K Hecker Michael M Becher Dörte D

Journal of proteome research 20150819 9

Staphylococcal biofilms are associated with persistent infections due to their capacity to protect bacteria against the host's immune system and antibiotics. Cell-surface-associated proteins are of great importance during biofilm formation. In the present study, an optimized biotinylation approach for quantitative GeLC-MS-based analysis of the staphylococcal cell-surface proteome was applied and the cytoplasmic protein fraction was analyzed to elucidate proteomic differences between colony biofi ...[more]

PMID: 26152824

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A type 2C protein phosphatase activates high-affinity nitrate uptake by directly dephosphorylating NRT2.1 in Arabidopsis

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