ArticleThe Journal of biological chemistry2008
Identification of ligand specificity determinants in AgrC, the Staphylococcus aureus quorum-sensing receptor.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 91 citations in OpenAlex.
- Hijacking the signal: a critical evaluation of quorum sensing inhibitors as a next-generation approach against Staphylococcus aureus.Cell communication and signaling : CCS · 2026Review
- Molecular Mechanisms of Virulence Regulation inAccounts of chemical research · 2025Article
- Determinants of maturation of theJournal of bacteriology · 2024Article
- Mutation of the peptide-regulated transcription factor ComR for amidated peptide specificity and heterologous function inMicrobiology spectrum · 2024Article
- Quorum-sensingeLife · 2024Article
- Quorum-sensingbioRxiv : the preprint server for biology · 2024Article
- - Invited Review - Chemical signalling within the rumen microbiome.Animal bioscience · 2024Article
- Deciphering agr quorum sensing in Staphylococcus aureus: insights and therapeutic prospects.Molecular biology reports · 2024Review
- Quorum-sensing, intra- and inter-species competition in the staphylococci.Microbiology (Reading, England) · 2023Review
- Chemical and biomolecular insights into theIsrael journal of chemistry · 2023Article
- Role of Staphylococcus aureus Formate Metabolism during Prosthetic Joint Infection.Infection and immunity · 2022Article
- Biofilms and Benign Colonic Diseases.International journal of molecular sciences · 2022Review
- Engineering ofInternational journal of molecular sciences · 2022Article
- Characterization of MroQ-Dependent Maturation and Export of the Staphylococcus aureus Accessory Gene Regulatory System Autoinducing Peptide.Infection and immunity · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Two-Component Systems ofGenes · 2021Review
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021Review
- The cytoplasmic loops of AgrC contribute to the quorum-sensing activity of Staphylococcus aureus.Journal of microbiology (Seoul, Korea) · 2021Article
- A Bacterial Tower of Babel: Quorum-Sensing Signaling Diversity and Its Evolution.Annual review of microbiology · 2020Review
Corrections and comments
- Erratum issuedChen, John [added]
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Activation of the agr system, a major regulator of staphylococcal virulence, is initiated by the binding of a specific autoinducing peptide (AIP) to the extracellular domain of AgrC, a classical receptor histidine protein kinase. There are four known agr specificity groups in Staphylococcus aureus, and we have previously localized the determinant of AIP receptor specificity to the C-terminal half of the AgrC sensor domain. We have now identified the specific amino acid residues that determine ligand activation specificity for agr groups I and IV, the two most closely related. Comparison of the AgrC-I and AgrC-IV sequences revealed a set of five divergent residues in the region of the second extracellular loop of the receptor that could be responsible. Accordingly, we exchanged these residues between AgrC-I and AgrC-IV and tested the resulting constructs for activation by the respective AIPs, measuring activation kinetics with a transcriptional fusion of blaZ to the principal agr promoter, P3. Exchange of all five residues caused a complete switch in receptor specificity. Replacement of two of the AgrC-IV residues by the corresponding residues in AgrC-I caused the receptor to be activated by AIP-I nearly as well as the wild type AgrC-I receptor. Replacement of two different AgrC-I residues by the corresponding AgrC-IV residues broadened receptor recognition specificity to include both AIPs. Various types of intermediate activity were observed with other replacement mutations. Preliminary characterization of the AgrC-I-AIP-I interaction suggests that ligand specificity may be sterically determined.
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Registered trials
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.