ArticleProceedings of the National Academy of Sciences of the United States of America2014
Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 140 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
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- Neutrophil Elastase Limits Spread of Staphylococcus aureus during Skin Infection.The Journal of infectious diseases · 2025Article
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- Exploring the involvement of serine proteases in neutrophil extracellular traps: a review of mechanisms and implications.Cell death & disease · 2025Review
- Extracellular adherence proteins reduce matrix porosity and enhanceInfection and immunity · 2025Article
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- Matrix porosity is associated withbioRxiv : the preprint server for biology · 2024Article
- The mononuclear phagocyte system obscures the accurate diagnosis of infected joint replacements.Journal of translational medicine · 2024Article
- New advances in understanding inhibition of myeloperoxidase and neutrophil serine proteases by two families of staphylococcal innate immune evasion proteins.Archives of biochemistry and biophysics · 2024Review
- Staphylococcal peroxidase inhibitor (SPIN): Residue-level investigation of the helical bundle domain.Archives of biochemistry and biophysics · 2024Article
- Interactions of Neutrophils with the Polymeric Molecular Components of the Biofilm Matrix in the Context of Implant-Associated Bone and Joint Infections.International journal of molecular sciences · 2023Review
- GFP fusions of Sec-routed extracellular proteins inMicrobial cell (Graz, Austria) · 2023Article
- Complete non-proline backbone resonance assignments of the S. aureus neutrophil serine protease inhibitor, EapH1.Biomolecular NMR assignments · 2023Article
- Staphylococcus aureus host interactions and adaptation.Nature reviews. Microbiology · 2023Review
- HowInternational journal of molecular sciences · 2023Review
- Soluble Signal Inhibitory Receptor on Leukocytes-1 Is Released from Activated Neutrophils by Proteinase 3 Cleavage.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- A genetic regulatory see-saw of biofilm and virulence in MRSA pathogenesis.Frontiers in microbiology · 2023Review
20 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 7 institutions in 3 countries.
Funding
Abstract
Neutrophils are indispensable for clearing infections with the prominent human pathogen Staphylococcus aureus. Here, we report that S. aureus secretes a family of proteins that potently inhibits the activity of neutrophil serine proteases (NSPs): neutrophil elastase (NE), proteinase 3, and cathepsin G. The NSPs, but not related serine proteases, are specifically blocked by the extracellular adherence protein (Eap) and the functionally orphan Eap homologs EapH1 and EapH2, with inhibitory-constant values in the low-nanomolar range. Eap proteins are together essential for NSP inhibition by S. aureus in vitro and promote staphylococcal infection in vivo. The crystal structure of the EapH1/NE complex showed that Eap molecules constitute a unique class of noncovalent protease inhibitors that occlude the catalytic cleft of NSPs. These findings increase our insights into the complex pathogenesis of S. aureus infections and create opportunities to design novel treatment strategies for inflammatory conditions related to excessive NSP activity.
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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.