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• W2040443588 endingPage "5050" @default.
• W2040443588 startingPage "5041" @default.
• W2040443588 abstract "ABSTRACT Protein turnover is a key process for bacterial survival mediated by intracellular proteases. Proteolytic degradation reduces the levels of unfolded and misfolded peptides that accumulate in the cell during stress conditions. Three intracellular proteases, ClpP, HslV, and FtsH, have been identified in the Gram-positive bacterium Staphylococcus aureus , a pathogen responsible for significant morbidity and mortality worldwide. Consistent with their crucial role in protein turnover, ClpP, HslV, and FtsH affect a number of cellular processes, including metabolism, stress responses, and virulence. The ClpP protease is believed to be the principal degradation machinery in S. aureus . This study sought to identify the effect of the Clp protease on the i ron-regulated s urface d eterminant (Isd) system, which extracts heme-iron from host hemoglobin during infection and is critical to S. aureus pathogenesis. Inactivation of components of the Clp protease alters abundance of several Isd proteins, including the hemoglobin receptor IsdB. Furthermore, the observed changes in IsdB abundance are the result of transcriptional regulation, since transcription of isdB is decreased by clpP or clpX inactivation. In contrast, inactivation of clpC enhances isdB transcription and protein abundance. Loss of clpP or clpX impairs host hemoglobin binding and utilization and results in severe virulence defects in a systemic mouse model of infection. These findings suggest that the Clp proteolytic system is important for regulating nutrient iron acquisition in S. aureus . The Clp protease and Isd complex are widely conserved in bacteria; therefore, these data reveal a novel Clp-dependent regulation pathway that may be present in other bacterial pathogens." @default.
• W2040443588 created "2016-06-24" @default.
• W2040443588 creator A5011093243 @default.
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• W2040443588 creator A5044897229 @default.
• W2040443588 creator A5047092331 @default.
• W2040443588 creator A5082616273 @default.
• W2040443588 date "2013-11-15" @default.
• W2040443588 modified "2023-10-16" @default.
• W2040443588 title "Regulation of Host Hemoglobin Binding by the Staphylococcus aureus Clp Proteolytic System" @default.
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• W2040443588 doi "https://doi.org/10.1128/jb.00505-13" @default.
• W2040443588 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3811588" @default.
• W2040443588 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23995637" @default.
• W2040443588 hasPublicationYear "2013" @default.
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