ArticlePLoS pathogens2015
The extracytoplasmic linker peptide of the sensor protein SaeS tunes the kinase activity required for staphylococcal virulence in response to host signals.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 57 citations in OpenAlex.
- Differential pathogenic and commensal response ofJournal of bacteriology · 2026Article
- An anti-adhesive compound modulating the production of Staphylococcus aureus cell wall-anchored proteins.Nature communications · 2026Article
- A novel SaeS-targeting antivirulence antagonist screened against methicillin-resistantFrontiers in cellular and infection microbiology · 2026Article
- Pyrimidine sufficiency is required for Sae two-component system signaling inJournal of bacteriology · 2025Article
- Human neutrophil defensin-1 binding increases histidine kinase activity of SaeS inBiochemistry and biophysics reports · 2025Article
- CodY controls the SaeR/S two-component system by modulating branched-chain fatty acid synthesis inJournal of bacteriology · 2024Article
- SaeR as a novel target for antivirulence therapy againstEmerging microbes & infections · 2023Article
- The Small Protein ScrA Influences Staphylococcus aureus Virulence-Related Processes via the SaeRS System.Microbiology spectrum · 2023Article
- Cell division protein FtsK coordinates bacterial chromosome segregation and daughter cell separation in Staphylococcus aureus.The EMBO journal · 2023Article
- CommensalACS omega · 2023Article
- Regulation of Bacterial Two-Component Systems by Cardiolipin.Infection and immunity · 2023Article
- Analysis of the Presence of the Virulence and Regulation Genes fromInternational journal of environmental research and public health · 2023Article
- Identification of an antivirulence agent targeting the master regulator of virulence genes inFrontiers in cellular and infection microbiology · 2023Article
- Article
- Virulence adaption to environment promotes the age-dependent nasal colonization ofEmerging microbes & infections · 2022Article
- Molybdopterin biosynthesis pathway contributes to the regulation of SaeRS two-component system by ClpP inVirulence · 2022Article
- Regulation of the Sae Two-Component System by Branched-Chain Fatty Acids in Staphylococcus aureus.mBio · 2022Article
- Revisiting the Role of VraTSR inJournal of bacteriology · 2022Article
- Two-Component Systems ofGenes · 2021Review
- The Sensor Histidine Kinase ArlS Is Necessary for Staphylococcus aureus To Activate ArlR in Response to Nutrient Availability.Journal of bacteriology · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial pathogens often employ two-component systems (TCSs), typically consisting of a sensor kinase and a response regulator, to control expression of a set of virulence genes in response to changing host environments. In Staphylococcus aureus, the SaeRS TCS is essential for in vivo survival of the bacterium. The intramembrane-sensing histidine kinase SaeS contains, along with a C-terminal kinase domain, a simple N-terminal domain composed of two transmembrane helices and a nine amino acid-long extracytoplasmic linker peptide. As a molecular switch, SaeS maintains low but significant basal kinase activity and increases its kinase activity in response to inducing signals such as human neutrophil peptide 1 (HNP1). Here we show that the linker peptide of SaeS controls SaeS's basal kinase activity and that the amino acid sequence of the linker peptide is highly optimized for its function. Without the linker peptide, SaeS displays aberrantly elevated kinase activity even in the absence of the inducing signal, and does not respond to HNP1. Moreover, SaeS variants with alanine substitution of the linker peptide amino acids exhibit altered basal kinase activity and/or irresponsiveness to HNP1. Biochemical assays reveal that those SaeS variants have altered autokinase and phosphotransferase activities. Finally, animal experiments demonstrate that the linker peptide-mediated fine tuning of SaeS kinase activity is critical for survival of the pathogen. Our results indicate that the function of the linker peptide in SaeS is a highly evolved feature with very optimized amino acid sequences, and we propose that, in other SaeS-like intramembrane sensing histidine kinases, the extracytoplasmic linker peptides actively fine-control their kinases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.