Staphylococcal superantigen‐like protein 13 activates neutrophils via formyl peptide receptor 2. (17th September 2018)

• Record Type: Journal Article
• Authors: Zhao, Yuxi; van Kessel, Kok P. M.; de Haas, Carla J. C.; Rogers, Malbert R. C.; van Strijp, Jos A. G.; Haas, Pieter‐Jan A.
• Is Part Of: Cellular microbiology. Volume 20:Number 11(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-09-17
• Subjects: activation -- FPR2 -- neutrophils -- SSL13 -- Staphylococcus aureus; Microbiology -- Periodicals; Cytology -- Periodicals; Host-parasite relationships -- Periodicals; Microbiology -- Periodicals; Cells -- Periodicals; Microbiologie -- Périodiques; Microbiologie; Relation hôte-parasite; Cytologie; Cellule; Réponse cellulaire; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); 579.05
• DOI: 10.1111/cmi.12941
• Languages: English
• ISSNs: 1462-5814

Abstract

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.