Linked Life Data

20108986

Source:http://linkedlifedata.com/resource/pubmed/id/20108986

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-3-5
pubmed:abstractText
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 (14)N(15)N 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1535-3907
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1579-90
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
pubmed:affiliation
Institute for Microbiology, Ernst-Moritz-Arndt-University Greifswald, Greifswald, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't