SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.

The Staphylococcus aureus regulatory saePQRS system controls the expression of numerous virulence factors, including extracellular adherence protein (Eap), which amongst others facilitates invasion of host cells. The saePQRS operon codes for 4 proteins: the histidine kinase SaeS, the response regula...

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Autores principales:	Phuti E Makgotlho, Gabriella Marincola, Daniel Schäfer, Qian Liu, Taeok Bae, Tobias Geiger, Elizabeth Wasserman, Christiane Wolz, Wilma Ziebuhr, Bhanu Sinha
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/07e34f462dfc4358805254495d13e509
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spelling	oai:doaj.org-article:07e34f462dfc4358805254495d13e5092021-11-18T08:58:49ZSDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.1932-620310.1371/journal.pone.0071644https://doaj.org/article/07e34f462dfc4358805254495d13e5092013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23977102/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The Staphylococcus aureus regulatory saePQRS system controls the expression of numerous virulence factors, including extracellular adherence protein (Eap), which amongst others facilitates invasion of host cells. The saePQRS operon codes for 4 proteins: the histidine kinase SaeS, the response regulator SaeR, the lipoprotein SaeP and the transmembrane protein SaeQ. S. aureus strain Newman has a single amino acid substitution in the transmembrane domain of SaeS (L18P) which results in constitutive kinase activity. SDS was shown to be one of the signals interfering with SaeS activity leading to inhibition of the sae target gene eap in strains with SaeS(L) but causing activation in strains containing SaeS(P). Here, we analyzed the possible involvement of the SaeP protein and saePQ region in SDS-mediated sae/eap expression. We found that SaePQ is not needed for SDS-mediated SaeS signaling. Furthermore, we could show that SaeS activity is closely linked to the expression of Eap and the capacity to invade host cells in a number of clinical isolates. This suggests that SaeS activity might be directly modulated by structurally non-complex environmental signals, as SDS, which possibly altering its kinase/phosphatase activity.Phuti E MakgotlhoGabriella MarincolaDaniel SchäferQian LiuTaeok BaeTobias GeigerElizabeth WassermanChristiane WolzWilma ZiebuhrBhanu SinhaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e71644 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Phuti E Makgotlho Gabriella Marincola Daniel Schäfer Qian Liu Taeok Bae Tobias Geiger Elizabeth Wasserman Christiane Wolz Wilma Ziebuhr Bhanu Sinha SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
description	The Staphylococcus aureus regulatory saePQRS system controls the expression of numerous virulence factors, including extracellular adherence protein (Eap), which amongst others facilitates invasion of host cells. The saePQRS operon codes for 4 proteins: the histidine kinase SaeS, the response regulator SaeR, the lipoprotein SaeP and the transmembrane protein SaeQ. S. aureus strain Newman has a single amino acid substitution in the transmembrane domain of SaeS (L18P) which results in constitutive kinase activity. SDS was shown to be one of the signals interfering with SaeS activity leading to inhibition of the sae target gene eap in strains with SaeS(L) but causing activation in strains containing SaeS(P). Here, we analyzed the possible involvement of the SaeP protein and saePQ region in SDS-mediated sae/eap expression. We found that SaePQ is not needed for SDS-mediated SaeS signaling. Furthermore, we could show that SaeS activity is closely linked to the expression of Eap and the capacity to invade host cells in a number of clinical isolates. This suggests that SaeS activity might be directly modulated by structurally non-complex environmental signals, as SDS, which possibly altering its kinase/phosphatase activity.
format	article
author	Phuti E Makgotlho Gabriella Marincola Daniel Schäfer Qian Liu Taeok Bae Tobias Geiger Elizabeth Wasserman Christiane Wolz Wilma Ziebuhr Bhanu Sinha
author_facet	Phuti E Makgotlho Gabriella Marincola Daniel Schäfer Qian Liu Taeok Bae Tobias Geiger Elizabeth Wasserman Christiane Wolz Wilma Ziebuhr Bhanu Sinha
author_sort	Phuti E Makgotlho
title	SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
title_short	SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
title_full	SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
title_fullStr	SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
title_full_unstemmed	SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.
title_sort	sds interferes with saes signaling of staphylococcus aureus independently of saepq.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/07e34f462dfc4358805254495d13e509
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SDS interferes with SaeS signaling of Staphylococcus aureus independently of SaePQ.

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