Phenol-soluble modulins form amyloids in contact with multiple surface chemistries

Functional amyloids are commonly produced by many microorganisms and their biological functions are numerous. Staphylococcus aureus can secrete a group of peptides named phenol-soluble modulins (PSMs) in their biofilm extracellular matrix. PSMs have been found inside biofilms both in their soluble f...

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Vydáno v:Biochimica et biophysica acta. General subjects Ročník 1867; číslo 11; s. 130450
Hlavní autoři: Marichal, Laurent, Bagnard, Lucie, Sire, Olivier, Vendrely, Charlotte, Bruckert, Franz, Weidenhaupt, Marianne
Médium: Journal Article
Jazyk:angličtina
Vydáno: Elsevier B.V 01.11.2023
Elsevier
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ISSN:0304-4165, 1872-8006, 1872-8006
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Shrnutí:Functional amyloids are commonly produced by many microorganisms and their biological functions are numerous. Staphylococcus aureus can secrete a group of peptides named phenol-soluble modulins (PSMs) in their biofilm extracellular matrix. PSMs have been found inside biofilms both in their soluble form and assembled into amyloid structures. Yet, the actual biological function of these amyloids has been highly debated. Here, we assessed the ability of PSMs to form amyloids in contact with different abiotic surfaces to unravel a potential unknown bioadhesive and/or biofilm stabilization function. We combined surface plasmon resonance imaging, fluorescence aggregation kinetics, and FTIR spectroscopy in order to evaluate the PSM adsorption as well as amyloid formation properties in the presence of various surface chemistries. Overall, PSMs adsorb even on low-binding surfaces, making them highly adaptable adsorbants in the context of bioadhesion. Moreover, the PSM aggregation potential to form amyloid aggregates is not impacted by the presence of the surface chemistries tested. This versatility regarding adsorption and amyloid formation may imply a possible role of PSMs in biofilm adhesion and/or structure integrity. •Phenol-soluble modulins can adsorb on highly different surface chemistries.•This adsorption versatility makes PSMs potential bioadhesion markers.•The amyloid formation of PSMs seems independent of surface chemistry.•A biological function for amyloid PSMs remains elusive.
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content type line 23
ISSN:0304-4165
1872-8006
1872-8006
DOI:10.1016/j.bbagen.2023.130450