The IL-8 protease SpyCEP is detrimental for Group A Streptococcus host-cells interaction and biofilm formation

Andreoni, Federica; Ogawa, Taiji; Ogawa, Mariko; Madon, Jerzy; Uchiyama, Satoshi; Schuepbach, Reto A.

doi:10.3389/fmicb.2014.00339

Cited by 16 publications

(20 citation statements)

References 31 publications

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“…However, virulence factors are energetically costly to produce, are advantageous only in specific circumstances, and if misregulated could have counter-productive consequences if immune-responses become stimulated [18,19]. Evolutionary biology predicts that complex virulence-regulatory and quorum-sensing pathways, such as those observed in GAS, may play key roles in bypassing bottlenecks such as the nasopharynx as well as in driving GAS speciation [6,20].…”

Section: Defining the Natural History Of Gasmentioning

confidence: 99%

Evolutionary Constraints Shaping Streptococcus pyogenes –Host Interactions

Wilkening

Federle

2017

Trends in Microbiology

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Research on the Gram-positive human-restricted pathogen Streptococcus pyogenes (Group A Streptococcus, GAS) has long focused on invasive illness, the most severe manifestations of GAS infection. Recent advances in descriptions of molecular mechanisms of GAS virulence, coupled with massive sequencing efforts of isolate genomes, have allowed the field to better understand the molecular and evolutionary changes leading to pandemic strains. These findings suggest it necessary to rethink the dogma involving GAS pathogenesis, and that the most productive avenues for research going forward may be investigations into GAS in its normal habitat, the nasopharynx, and its ability to either live with its host in an asymptomatic lifestyle or as an agent of superficial infections. This review will consider these advances, focusing on the natural history of GAS, the evolution of pandemic strains and novel roles for several key virulence factors that may allow the field to better understand their physiological role.

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Section: Defining the Natural History Of Gasmentioning

confidence: 99%

Evolutionary Constraints Shaping Streptococcus pyogenes –Host Interactions

Wilkening

Federle

2017

Trends in Microbiology

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“…Furthermore, the inclusion of non‐standard amino acids is another strategy to increase the peptide stability against proteolytic cleavage . Also, it might be of interest to study potential peptide oligomerization, as it could further increase GAG binding . These strategies might facilitate the impairment of the chemokine‐mediated neutrophil recruitment to ameliorate the injury associated with neutrophil‐mediated inflammation, such as in ischaemia reperfusion injury during transplantation, or in rheumatoid arthritis …”

Section: Discussionmentioning

confidence: 99%

“…76 Also, it might be of interest to study potential peptide oligomerization, as it could further increase GAG binding. 29,42,43,77,78 These strategies might facilitate the impairment of the chemokine-mediated neutrophil recruitment to ameliorate the injury associated with neutrophil-mediated inflammation, such as in ischaemia reperfusion injury during transplantation, or in rheumatoid arthritis. 79 Mice express only CXCL8 homologues, KC/CXCL1 and MIP-2/CXCL2.…”

Section: Discussionmentioning

confidence: 99%

A C‐terminal CXCL8 peptide based on chemokine–glycosaminoglycan interactions reduces neutrophil adhesion and migration during inflammation

et al. 2019

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Summary Leucocyte recruitment is critical during many acute and chronic inflammatory diseases. Chemokines are key mediators of leucocyte recruitment during the inflammatory response, by signalling through specific chemokine G‐protein‐coupled receptors (GPCRs). In addition, chemokines interact with cell‐surface glycosaminoglycans (GAGs) to generate a chemotactic gradient. The chemokine interleukin‐8/CXCL8, a prototypical neutrophil chemoattractant, is characterized by a long, highly positively charged GAG‐binding C‐terminal region, absent in most other chemokines. To examine whether the CXCL8 C‐terminal peptide has a modulatory role in GAG binding during neutrophil recruitment, we synthesized the wild‐type CXCL8 C‐terminal [CXCL8 (54–72)] (Peptide 1), a peptide with a substitution of glutamic acid (E) 70 with lysine (K) (Peptide 2) to increase positive charge; and also, a scrambled sequence peptide (Peptide 3). Surface plasmon resonance showed that Peptide 1, corresponding to the core CXCL8 GAG‐binding region, binds to GAG but Peptide 2 binding was detected at lower concentrations. In the absence of cellular GAG, the peptides did not affect CXCL8‐induced calcium signalling or neutrophil chemotaxis along a diffusion gradient, suggesting no effect on GPCR binding. All peptides equally inhibited neutrophil adhesion to endothelial cells under physiological flow conditions. Peptide 2, with its greater positive charge and binding to polyanionic GAG, inhibited CXCL8‐induced neutrophil transendothelial migration. Our studies suggest that the E70K CXCL8 peptide, may serve as a lead molecule for further development of therapeutic inhibitors of neutrophil‐mediated inflammation based on modulation of chemokine–GAG binding.

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“…In addition, bacterial aggregates resembling biofilms were observed in histologic samples from mouse and humans, as previously shown. 11,19,20 At our hospital, as is the case for many other centers, histologic samples are, in contrast to microbiology samples, rarely taken from NF patients for further analysis. Thus, in >50% of the patients with NF no histology was available.…”

Section: Discussionmentioning

confidence: 99%

Human Streptococcal Necrotizing Fasciitis Histopathology Mirrored in a Murine Model

Keller

Andreoni

Reiber

et al. 2018

The American Journal of Pathology

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Streptococcal necrotizing fasciitis (NF) causes high morbidity and mortality despite state-of-the-art therapy. Low incidence and rapid disease progression, necessitating immediate initiation of therapy, have proven challenging aspects for setting up prospective randomized trials. This has resulted in little therapeutic progress over the past decade. The validation of reliable murine NF models to study both pathogenesis and optimized therapeutic regimens of streptococcal NF are thus essential. In this study, we characterized a murine NF model and compared the pathology with an in-depth tissue analysis of streptococcal NF in patients. We found that the streptococcal murine NF model closely reflected all histologic characteristics encountered in human streptococcal NF. This murine NF model helps understanding of human NF pathology better in a time-dependent manner and will allow studying novel therapeutic options in the future.

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The IL-8 protease SpyCEP is detrimental for Group A Streptococcus host-cells interaction and biofilm formation

Cited by 16 publications

References 31 publications

Evolutionary Constraints Shaping Streptococcus pyogenes –Host Interactions

Evolutionary Constraints Shaping Streptococcus pyogenes –Host Interactions

A C‐terminal CXCL8 peptide based on chemokine–glycosaminoglycan interactions reduces neutrophil adhesion and migration during inflammation

Human Streptococcal Necrotizing Fasciitis Histopathology Mirrored in a Murine Model

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