ArticleThe Journal of biological chemistry2015
Recognition of bacterial signal peptides by mammalian formyl peptide receptors: a new mechanism for sensing pathogens.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 97 citations in OpenAlex.
- Pooled it
- Assessing Vancomycin-Formyl Peptide Conjugate Binding to the Surface of Resistant Staphylococcus aureus via Flow Cytometry.Chembiochem : a European journal of chemical biology · 2026Article
- Integrated Phylogenomics and Expression Profiling of the Peptide Deformylase Gene Family inCurrent issues in molecular biology · 2026Article
- Cross-Platform Biosensing of Immune Receptors Using Peptide-Functionalized Graphene.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Molecular insight into transcriptome profiling of aerobic exercise induced changes in aged skeletal muscle.npj aging · 2026Article
- Assessing the potential of bacterial signal peptides for radiopharmaceutical applications.Scientific reports · 2025Article
- Fragments of viral surface proteins modulate innate immune responses via formyl peptide receptors.iScience · 2025Article
- Antimicrobial Peptide Signaling in Skin Diseases.JID innovations : skin science from molecules to population health · 2025Review
- TheFrontiers in immunology · 2025Review
- Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors.Genome biology and evolution · 2023Article
- Sensing and avoiding sick conspecifics requires Gαi2BMC biology · 2023Article
- Developmental and homeostatic signaling transmitted by the G-protein coupled receptor FPR2.International immunopharmacology · 2023Review
- Nocardia rubra cell-wall skeleton activates an immune response in cervical tissueFrontiers in immunology · 2023Article
- Promiscuous Receptors and Neuroinflammation: The Formyl Peptide Class.Life (Basel, Switzerland) · 2022Review
- Roles of mitochondrial genetics in cancer metastasis.Trends in cancer · 2022Review
- Macrophages disseminate pathogen associated molecular patterns through the direct extracellular release of the soluble content of their phagolysosomes.Nature communications · 2022Article
- Selective Display of a Chemoattractant Agonist on Cancer Cells Activates the Formyl Peptide Receptor 1 on Immune Cells.Chembiochem : a European journal of chemical biology · 2022Article
- Mitochondrial and metabolic dysfunction in ageing and age-related diseases.Nature reviews. Endocrinology · 2022Review
- Anti-Inflammatory and Active Biological Properties of the Plant-Derived Bioactive Compounds Luteolin and Luteolin 7-Glucoside.Nutrients · 2022Review
- Neutrophils discriminate live from dead bacteria by integrating signals initiated by Fprs and TLRs.The EMBO journal · 2022Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formyl peptide receptors (FPRs) are G-protein-coupled receptors that function as chemoattractant receptors in innate immune responses. Here we perform systematic structure-function analyses of FPRs from six mammalian species using structurally diverse FPR peptide agonists and identify a common set of conserved agonist properties with typical features of pathogen-associated molecular patterns. Guided by these results, we discover that bacterial signal peptides, normally used to translocate proteins across cytoplasmic membranes, are a vast family of natural FPR agonists. N-terminally formylated signal peptide fragments with variable sequence and length activate human and mouse FPR1 and FPR2 at low nanomolar concentrations, thus establishing FPR1 and FPR2 as sensitive and broad signal peptide receptors. The vomeronasal receptor mFpr-rs1 and its sequence orthologue hFPR3 also react to signal peptides but are much more narrowly tuned in signal peptide recognition. Furthermore, all signal peptides examined here function as potent activators of the innate immune system. They elicit robust, FPR-dependent calcium mobilization in human and mouse leukocytes and trigger a range of classical innate defense mechanisms, such as the production of reactive oxygen species, metalloprotease release, and chemotaxis. Thus, bacterial signal peptides constitute a novel class of immune activators that are likely to contribute to mammalian immune defense against bacteria. This evolutionarily conserved detection mechanism combines structural promiscuity with high specificity and enables discrimination between bacterial and eukaryotic signal sequences. With at least 175,542 predicted sequences, bacterial signal peptides represent the largest and structurally most heterogeneous class of G-protein-coupled receptor agonists currently known for the innate immune system.
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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.