ArticleCellular microbiology2018
Staphylococcal superantigen-like protein 13 activates neutrophils via formyl peptide receptor 2.
Article in Cellular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Integrated multi-omics reveals coordinatedmSystems · 2026Article
- α-hemolysin polymorphisms in methicillin-resistantbioRxiv : the preprint server for biology · 2025Article
- Review
- Remodeling of Paranasal Sinuses Mucosa Functions in Response to Biofilm-Induced Inflammation.Journal of inflammation research · 2024Review
- Staphylococcal superantigen-like protein 10 enhances the amyloidogenic biofilm formation in Staphylococcus aureus.BMC microbiology · 2023Article
- Isolation and functional analysis of phage-displayed antibody fragments targeting the staphylococcal superantigen-like proteins.MicrobiologyOpen · 2023Article
- Staphylococcus aureus host interactions and adaptation.Nature reviews. Microbiology · 2023Review
- The Influence of Antibiotic Resistance on Innate Immune Responses toAntibiotics (Basel, Switzerland) · 2022Review
- Multiple Domains of Staphylococcal Superantigen-like Protein 11 (SSL11) Contribute to Neutrophil Inhibition.Biochemistry · 2022Article
- Bacteriophage: A new therapeutic player to combat neutrophilic inflammation in chronic airway diseases.Frontiers in medicine · 2022Review
- Genomic analysis of European bovine Staphylococcus aureus from clinical versus subclinical mastitis.Scientific reports · 2020Article
- Progress in Model Systems of Cystic Fibrosis Mucosal Inflammation to Understand Aberrant Neutrophil Activity.Frontiers in immunology · 2020Review
- Staphylococcal superantigen-like protein 13 activates neutrophils via formyl peptide receptor 2.Cellular microbiology · 2018Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcal superantigen-like (SSL) proteins, one of the major virulence factor families produced by Staphylococcus aureus, were previously demonstrated to be immune evasion molecules that interfere with a variety of innate immune defences. However, in contrast to characterised SSLs, which inhibit immune functions, we show that SSL13 is a strong activator of neutrophils via the formyl peptide receptor 2 (FPR2). Moreover, our data show that SSL13 acts as a chemoattractant and induces degranulation and oxidative burst in neutrophils. As with many other staphylococcal immune evasion proteins, SSL13 shows a high degree of human specificity. SSL13 is not able to efficiently activate mouse neutrophils, hampering in vivo experiments. In conclusion, SSL13 is a neutrophil chemoattractant and activator that acts via FPR2. Therefore, SSL13 is a unique SSL member that does not belong to the immune evasion class but is a pathogen alarming molecule. Our study provides a new concept of SSLs; SSLs not only inhibit host immune processes but also recruit human neutrophils to the site of infection. This new insight allows us to better understand complex interactions between host and S. aureus pathological processes.
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