Cargando…
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2
The human formyl-peptide receptor 2 (FPR2/ALX) senses phenol-soluble modulin (PSM) peptide toxins produced by pathogenic staphylococcal species and plays a crucial role in directing neutrophil influx during staphylococcal infection. However, it has remained unclear if FPR2 responds also to molecules...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386911/ https://www.ncbi.nlm.nih.gov/pubmed/22768166 http://dx.doi.org/10.1371/journal.pone.0039910 |
_version_ | 1782237031700627456 |
---|---|
author | Bloes, Dominik Alexander Otto, Michael Peschel, Andreas Kretschmer, Dorothee |
author_facet | Bloes, Dominik Alexander Otto, Michael Peschel, Andreas Kretschmer, Dorothee |
author_sort | Bloes, Dominik Alexander |
collection | PubMed |
description | The human formyl-peptide receptor 2 (FPR2/ALX) senses phenol-soluble modulin (PSM) peptide toxins produced by pathogenic staphylococcal species and plays a crucial role in directing neutrophil influx during staphylococcal infection. However, it has remained unclear if FPR2 responds also to molecules from other bacterial pathogens. Here we analyzed a variety of Gram-positive and Gram-negative pathogens and found that apart from staphylococci only certain enterococcal strains have the capacity to stimulate FPR2/ALX. Most of the analyzed Enterococcus faecium but only sporadic Enterococcus faecalis strains released FPR2/ALX-stimulating molecules leading to neutrophil calcium ion fluxes, chemotaxis, and complement receptor upregulation. Among ten test strains vancomycin-resistant E. faecium had a significantly higher capacity to stimulate FPR2/ALX than vancomycin-susceptible strains, suggesting an association of strong FPR2/ALX activation with health-care associated strains. The enterococcal FPR2/ALX agonists were found to be peptides or proteins, which appear, however, to be unrelated to staphylococcal PSMs in sequence and physicochemical properties. Enterococci are among the most frequent invasive bacterial pathogens but the basis of enterococcal virulence and immune activation has remained incompletely understood. Our study indicates that previously unrecognized proteinaceous agonists contribute to Enterococcus-host interaction and underscores the importance of FPR2/ALX in host defense against major endogenous bacterial pathogens. |
format | Online Article Text |
id | pubmed-3386911 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33869112012-07-05 Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 Bloes, Dominik Alexander Otto, Michael Peschel, Andreas Kretschmer, Dorothee PLoS One Research Article The human formyl-peptide receptor 2 (FPR2/ALX) senses phenol-soluble modulin (PSM) peptide toxins produced by pathogenic staphylococcal species and plays a crucial role in directing neutrophil influx during staphylococcal infection. However, it has remained unclear if FPR2 responds also to molecules from other bacterial pathogens. Here we analyzed a variety of Gram-positive and Gram-negative pathogens and found that apart from staphylococci only certain enterococcal strains have the capacity to stimulate FPR2/ALX. Most of the analyzed Enterococcus faecium but only sporadic Enterococcus faecalis strains released FPR2/ALX-stimulating molecules leading to neutrophil calcium ion fluxes, chemotaxis, and complement receptor upregulation. Among ten test strains vancomycin-resistant E. faecium had a significantly higher capacity to stimulate FPR2/ALX than vancomycin-susceptible strains, suggesting an association of strong FPR2/ALX activation with health-care associated strains. The enterococcal FPR2/ALX agonists were found to be peptides or proteins, which appear, however, to be unrelated to staphylococcal PSMs in sequence and physicochemical properties. Enterococci are among the most frequent invasive bacterial pathogens but the basis of enterococcal virulence and immune activation has remained incompletely understood. Our study indicates that previously unrecognized proteinaceous agonists contribute to Enterococcus-host interaction and underscores the importance of FPR2/ALX in host defense against major endogenous bacterial pathogens. Public Library of Science 2012-06-29 /pmc/articles/PMC3386911/ /pubmed/22768166 http://dx.doi.org/10.1371/journal.pone.0039910 Text en This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Bloes, Dominik Alexander Otto, Michael Peschel, Andreas Kretschmer, Dorothee Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title |
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title_full |
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title_fullStr |
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title_full_unstemmed |
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title_short |
Enterococcus faecium Stimulates Human Neutrophils via the Formyl-Peptide Receptor 2 |
title_sort | enterococcus faecium stimulates human neutrophils via the formyl-peptide receptor 2 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386911/ https://www.ncbi.nlm.nih.gov/pubmed/22768166 http://dx.doi.org/10.1371/journal.pone.0039910 |
work_keys_str_mv | AT bloesdominikalexander enterococcusfaeciumstimulateshumanneutrophilsviatheformylpeptidereceptor2 AT ottomichael enterococcusfaeciumstimulateshumanneutrophilsviatheformylpeptidereceptor2 AT peschelandreas enterococcusfaeciumstimulateshumanneutrophilsviatheformylpeptidereceptor2 AT kretschmerdorothee enterococcusfaeciumstimulateshumanneutrophilsviatheformylpeptidereceptor2 |