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Published on: December 27, 2016
Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure
Patrizia Marinelli1, Irantzu Pallares1,2, Susanna Navarro1,2
1Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.
Abstract:
The opportunistic pathogen Staphylococcus aureus is recognized as one of the most frequent causes of biofilm-associated infections. The recently discovered phenol soluble modulins (PSMs) are small α-helical amphipathic peptides that act as the main molecular effectors of staphylococcal biofilm maturation, promoting the formation of an extracellular fibril structure with amyloid-like properties. Here, we combine computational, biophysical and in cell analysis to address the specific contribution of individual PSMs to biofilm structure. We demonstrate that despite their highly similar sequence and structure, contrary to what it was previously thought, not all PSMs participate in amyloid fibril formation. A balance of hydrophobic/hydrophilic forces and helical propensity seems to define the aggregation propensity of PSMs and control their assembly and function. This knowledge would allow to target specifically the amyloid properties of these peptides. In this way, we show that Epigallocatechin-3-gallate (EGCG), the principal polyphenol in green tea, prevents the assembly of amyloidogenic PSMs and disentangles their preformed amyloid fibrils.
Insights
Phenol soluble modulins (PSMs) are key to Staphylococcus aureus biofilm structure. Not all PSMs form amyloid fibrils; their aggregation depends on sequence and structure, offering new therapeutic targets.
Area of Science:
- Microbiology
- Biophysics
- Structural Biology
Background:
- Staphylococcus aureus is a major cause of biofilm-associated infections.
- Phenol soluble modulins (PSMs) are critical effectors in staphylococcal biofilm maturation, forming amyloid-like fibrils.
- Understanding individual PSM contributions to biofilm structure is crucial for developing targeted therapies.
Purpose of the Study:
- To investigate the specific role of individual PSMs in Staphylococcus aureus biofilm formation.
- To determine the factors governing the aggregation propensity and function of different PSMs.
- To explore potential therapeutic strategies targeting PSM amyloid formation.
Main Methods:
- Computational analysis of PSM sequences and structures.
- Biophysical techniques to assess peptide aggregation and fibril formation.
- In-cell studies to observe PSM behavior within bacterial biofilms.
Main Results:
- Despite sequence and structural similarities, not all PSMs contribute to amyloid fibril formation.
- Hydrophobic/hydrophilic balance and helical propensity dictate PSM aggregation and function.
- Epigallocatechin-3-gallate (EGCG) inhibits amyloidogenic PSM assembly and disassembles preformed fibrils.
Conclusions:
- PSM function in biofilm structure is more complex than previously assumed, with specific peptides driving amyloid formation.
- The aggregation propensity of PSMs is governed by intrinsic physicochemical properties.
- EGCG presents a potential therapeutic agent to disrupt Staphylococcus aureus biofilms by targeting PSM amyloid structures.
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