Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus

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Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus. / Farrand, Allison J; Friedman, David B; Reniere, Michelle L; Ingmer, Hanne; Frees, Dorte; Skaar, Eric P.

I: Pathogens and Disease, Bind 73, Nr. 3, ftv004, 04.2015.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Farrand, AJ, Friedman, DB, Reniere, ML, Ingmer, H, Frees, D & Skaar, EP 2015, 'Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus', Pathogens and Disease, bind 73, nr. 3, ftv004. https://doi.org/10.1093/femspd/ftv004

APA

Farrand, A. J., Friedman, D. B., Reniere, M. L., Ingmer, H., Frees, D., & Skaar, E. P. (2015). Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus. Pathogens and Disease, 73(3), [ftv004]. https://doi.org/10.1093/femspd/ftv004

Vancouver

Farrand AJ, Friedman DB, Reniere ML, Ingmer H, Frees D, Skaar EP. Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus. Pathogens and Disease. 2015 apr.;73(3). ftv004. https://doi.org/10.1093/femspd/ftv004

Author

Farrand, Allison J ; Friedman, David B ; Reniere, Michelle L ; Ingmer, Hanne ; Frees, Dorte ; Skaar, Eric P. / Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus. I: Pathogens and Disease. 2015 ; Bind 73, Nr. 3.

Bibtex

@article{e91b4b7b0930452eb1ef79c29051bbfd,
title = "Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus",
abstract = "Staphylococcus aureus is a frequent human pathogen that is capable of causing a wide range of life-threatening infections. A promising antibacterial target is the Clp proteolytic system, which performs the vital function of maintaining protein turnover within the cell. This system primarily impacts the bacterial response to various stresses by degrading specific proteins but can also regulate a number of physiological processes through protein degradation. A critical stress to which S. aureus must adapt during infection of a vertebrate host is nutrient iron limitation. We have previously shown that the Clp system impacts expression of genes required for heme-iron acquisition during iron limitation and is required for staphylococcal infection. Based on these data, we sought to further define the Clp-dependent impact on S. aureus during iron limitation by characterizing the proteomic profiles of mutants inactivated for components of the Clp protease, including ClpP, ClpC and ClpX, in high- and low-iron conditions. Our results reveal numerous proteins altered in abundance in the clp mutants and provide new insights into the staphylococcal proteolytic network during nutrient iron limitation.",
keywords = "Faculty of Health and Medical Sciences, protein, degradation, 2D-DIGE",
author = "Farrand, {Allison J} and Friedman, {David B} and Reniere, {Michelle L} and Hanne Ingmer and Dorte Frees and Skaar, {Eric P}",
note = "{\textcopyright} FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.",
year = "2015",
month = apr,
doi = "10.1093/femspd/ftv004",
language = "English",
volume = "73",
journal = "FEMS Immunology and Medical Microbiology",
issn = "2049-632X",
publisher = "Oxford University Press",
number = "3",

}

RIS

TY - JOUR

T1 - Proteomic analyses of iron-responsive, Clp-dependent changes in Staphylococcus aureus

AU - Farrand, Allison J

AU - Friedman, David B

AU - Reniere, Michelle L

AU - Ingmer, Hanne

AU - Frees, Dorte

AU - Skaar, Eric P

N1 - © FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

PY - 2015/4

Y1 - 2015/4

N2 - Staphylococcus aureus is a frequent human pathogen that is capable of causing a wide range of life-threatening infections. A promising antibacterial target is the Clp proteolytic system, which performs the vital function of maintaining protein turnover within the cell. This system primarily impacts the bacterial response to various stresses by degrading specific proteins but can also regulate a number of physiological processes through protein degradation. A critical stress to which S. aureus must adapt during infection of a vertebrate host is nutrient iron limitation. We have previously shown that the Clp system impacts expression of genes required for heme-iron acquisition during iron limitation and is required for staphylococcal infection. Based on these data, we sought to further define the Clp-dependent impact on S. aureus during iron limitation by characterizing the proteomic profiles of mutants inactivated for components of the Clp protease, including ClpP, ClpC and ClpX, in high- and low-iron conditions. Our results reveal numerous proteins altered in abundance in the clp mutants and provide new insights into the staphylococcal proteolytic network during nutrient iron limitation.

AB - Staphylococcus aureus is a frequent human pathogen that is capable of causing a wide range of life-threatening infections. A promising antibacterial target is the Clp proteolytic system, which performs the vital function of maintaining protein turnover within the cell. This system primarily impacts the bacterial response to various stresses by degrading specific proteins but can also regulate a number of physiological processes through protein degradation. A critical stress to which S. aureus must adapt during infection of a vertebrate host is nutrient iron limitation. We have previously shown that the Clp system impacts expression of genes required for heme-iron acquisition during iron limitation and is required for staphylococcal infection. Based on these data, we sought to further define the Clp-dependent impact on S. aureus during iron limitation by characterizing the proteomic profiles of mutants inactivated for components of the Clp protease, including ClpP, ClpC and ClpX, in high- and low-iron conditions. Our results reveal numerous proteins altered in abundance in the clp mutants and provide new insights into the staphylococcal proteolytic network during nutrient iron limitation.

KW - Faculty of Health and Medical Sciences

KW - protein

KW - degradation

KW - 2D-DIGE

U2 - 10.1093/femspd/ftv004

DO - 10.1093/femspd/ftv004

M3 - Journal article

C2 - 25743475

VL - 73

JO - FEMS Immunology and Medical Microbiology

JF - FEMS Immunology and Medical Microbiology

SN - 2049-632X

IS - 3

M1 - ftv004

ER -

ID: 144449049