The<i>sae</i>locus of<i>Staphylococcus aureus</i>encodes a two-component regulatory system

Giraudo, Ana T.; Calzolari, A.; Cataldi, Angel; Bogni, Cristina; Nagel, Rosa

doi:10.1111/j.1574-6968.1999.tb13707.x

Cited by 147 publications

(57 citation statements)

References 19 publications

(29 reference statements)

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“…SaeS is composed of 351 aa where His131 is the phosphorylation site [13]. As a sensor histidine kinase, its kinase activity determines the level of SaeR-P, the effector molecule of the SaeRS TCS.…”

Section: Components Of the Saers Tcsmentioning

confidence: 99%

“…For example, agr mutation reduced both the sae P1 promoter activity and the Sae mRNA level [13,14,15,79]. In the strain ISP479, a derivative of the strain 8325-4, an agr mutation greatly reduced the sae P3 promoter function in the 1.15 kb fragment upstream of saeR [80].…”

Section: Interaction With Other Regulatorsmentioning

confidence: 99%

“…For example, in the 2003 study by Giraudo et al [80], despite the fact that agr mutation abolished the promoter activity of sae P3 at OD 600 = 4, no significant changes were observed in the transcript profile analyzed by Northern blot. Moreover, in most studies, the effect of agr mutation on the sae expression was not confirmed by a complementation test [13,14,79]. Recently, Baroja et al showed that, in the strain MN8, the deletion of agr did not affect the transcription of saeR [73], further confirming the independence of Agr and Sae.…”

Section: Interaction With Other Regulatorsmentioning

confidence: 99%

“…The sae ( S. aureus exoprotein expression) locus, which encodes the SaeRS TCS, was identified by Giraudo et al in 1994 during their characterization of a Tn551 mutant for its defect in the production of exoproteins (e.g., α-hemolysin, β-hemolysin, nuclease, and coagulase) [12,13]. As with other typical TCSs, the signaling cascade in the SaeRS TCS starts when SaeS, the sensor histidine kinase, detects cognate environmental signals (e.g., human neutrophil peptides, HNPs) [14] and autophosphorylates at the conserved His131 residue.…”

Section: Introductionmentioning

confidence: 99%

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The SaeRS Two‐Component System of Staphylococcus aureus

Liu

Yeo

Bae

2016

Genes

175

195

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In the Gram-positive pathogenic bacterium Staphylococcus aureus, the SaeRS two-component system (TCS) plays a major role in controlling the production of over 20 virulence factors including hemolysins, leukocidins, superantigens, surface proteins, and proteases. The SaeRS TCS is composed of the sensor histidine kinase SaeS, response regulator SaeR, and two auxiliary proteins SaeP and SaeQ. Since its discovery in 1994, the sae locus has been studied extensively, and its contributions to staphylococcal virulence and pathogenesis have been well documented and understood; however, the molecular mechanism by which the SaeRS TCS receives and processes cognate signals is not. In this article, therefore, we review the literature focusing on the signaling mechanism and its interaction with other global regulators.

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Section: Components Of the Saers Tcsmentioning

confidence: 99%

Section: Interaction With Other Regulatorsmentioning

confidence: 99%

Section: Interaction With Other Regulatorsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The SaeRS Two‐Component System of Staphylococcus aureus

Liu

Yeo

Bae

2016

Genes

175

195

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“…The well-studied global and TCSs virulence regulators include Agr (Novick, 2003; Montgomery et al, 2010; Thoendel and Horswill, 2013), ArlRS (Fournier et al, 2001; Bronner et al, 2004; Liang et al, 2005), SaeRS (Giraudo et al, 1999; Liang et al, 2006; Voyich et al, 2009; Nygaard et al, 2010; Zurek et al, 2014; Liu et al, 2016), SarA (Chien et al, 1999; Cheung et al, 2008; Li et al, 2016; Loughran et al, 2016), and MgrA (Ballal et al, 2009; Gupta et al, 2015). …”

Section: Introductionmentioning

confidence: 99%

The SaeRS Two-Component System Controls Survival of Staphylococcus aureus in Human Blood through Regulation of Coagulase

Guo

Hall

Yang

et al. 2017

Front. Cell. Infect. Microbiol.

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The SaeRS two-component system plays important roles in regulation of key virulence factors and pathogenicity. In this study, however, we found that the deletion mutation of saeRS enhanced bacterial survival in human blood, whereas complementation of the mutant with SaeRS returned survival to wild-type levels. Moreover, these phenomena were observed in different MRSA genetic background isolates, including HA-MRSA WCUH29, CA-MRSA 923, and MW2. To elucidate which gene(s) regulated by SaeRS contribute to the effect, we conducted a series of complementation studies with selected known SaeRS target genes in trans. We found coagulase complementation abolished the enhanced survival of the SaeRS mutant in human blood. The coa and saeRS deletion mutants exhibited a similar survival phenotype in blood. Intriguingly, heterologous expression of coagulase decreased survival of S. epidermidis in human blood. Further, the addition of recombinant coagulase to blood significantly decreased the survival of S. aureus. Further, analysis revealed staphylococcal resistance to killing by hydrogen peroxide was partially dependent on the presence or absence of coagulase. Furthermore, complementation with coagulase, but not SaeRS, returned saeRS/coa double mutant survival in blood to wild-type levels. These data indicate SaeRS modulates bacterial survival in blood in coagulase-dependent manner. Our results provide new insights into the role of staphylococcal SaeRS and coagulase on bacterial survival in human blood.

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Extracellular proteins ofStaphylococcus aureus and the role of SarA andσB

et al. 2001

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Staphylococcus aureus synthesizes a large number of extracellular proteins that have been postulated to play a role in bacterial virulence. The proteomic approach was used to analyse the pattern of extracellular proteins of two different S. aureus strains, RN6390 and COL. Thirty-nine protein spots were identified by N-terminal sequencing or MALDI-TOF-MS. The differences of the extracellular protein patterns between both strains are striking. Among the 18 proteins identified in S. aureus COL there are nine proteins not yet discovered in S. aureus RN6390. These are enterotoxin B, leukotoxin D, enterotoxin, serin proteases (SplA and SplC), thermonuclease, an IgG binding protein and two so far unknown proteins in S. aureus with similarities to SceD precursor in Staphylococcus carnosus and to synergohymenotropic toxin precursor in Streptococcus intermedius. In contrast, lipase as well as staphylokinase identified in S. aureus RN6390 were not detectable in S. aureus COL under the same conditions. By using a regulatory mutant of sarA (ALC136) isogenic to strain RN6390 we identified five proteins positively regulated by SarA and 12 proteins negatively regulated by SarA. Besides V8 protease (StsP) and Hlb already described to be regulated by the sar locus new putatively sarA-dependent proteins were identified, e.g. glycerolester hydrolase and autolysin both down-regulated in the sarA mutant, and aureolysin, staphylokinase, staphopain and format tetrahydrofolate lyase up-regulated in the mutant. Moreover, the role of sigma B in expression of extracellular proteins was studied. Interestingly, we found 11 proteins at an enhanced level in a sigB mutant of S. aureus COL, among them enterotoxin B, alpha and beta hemolysin, serine proteases SplA and SplB, leukotoxin D, and staphopain homologues. The sigma B-dependent repression of gene expression occurs at the transcriptional level. Only one protein, SceD, was identified whose synthesis was down-regulated in the mutant indicating that its gene belongs to the sigma B-dependent general stress regulon.

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Thesaelocus ofStaphylococcus aureusencodes a two-component regulatory system

Cited by 147 publications

References 19 publications

The SaeRS Two‐Component System of Staphylococcus aureus

The SaeRS Two‐Component System of Staphylococcus aureus

The SaeRS Two-Component System Controls Survival of Staphylococcus aureus in Human Blood through Regulation of Coagulase

Extracellular proteins ofStaphylococcus aureus and the role of SarA andσB

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