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Rapid Generation of Amyloid from Native Proteins In vitro
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Do amyloid structures formed by Staphylococcus aureus phenol-soluble modulins have a biological function?

Yue Zheng1, Hwang-Soo Joo2, Vinod Nair3

  • 1Pathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, 50 South Drive, Bethesda, MD 20814, USA.

International Journal of Medical Microbiology : IJMM
|September 5, 2017
PubMed
Summary

Phenol-soluble modulins (PSMs) form amyloid fibrils, but this may not explain their roles in staphylococcal virulence or biofilm stability. PSM-DNA interactions offer an alternative explanation for biofilm effects.

Keywords:
AmyloidBiofilmPhenol-soluble modulinsStaphylococcus aureusToxin

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Phenol-soluble modulins (PSMs) are crucial virulence factors in Staphylococcus species.
  • Recent studies proposed that PSM amyloid formation contributes to cytolysis and biofilm stability.

Purpose of the Study:

  • To investigate the role of PSM amyloid formation in staphylococcal virulence and biofilm formation.
  • To explore alternative mechanisms for PSM-mediated biofilm stability.

Main Methods:

  • Electron microscopy and dye-binding assays to detect PSM amyloid formation.
  • Comparison of extracellular fibrous material production between wild-type and PSM-deficient strains.
  • Assessment of PSM derivatives' propensity to form amyloids and their correlation with cytolytic and pro-inflammatory activities.
  • Investigation of PSM interaction with DNA and DNase resistance.

Main Results:

  • PSM amyloid formation was confirmed, but no differences in extracellular fibril production were observed between wild-type and PSM-deficient strains.
  • No correlation was found between amyloid formation propensity and cytolytic or pro-inflammatory activities.
  • PSMs bind non-specifically to DNA, conferring DNase resistance, which explains biofilm stability without amyloid involvement.
  • High conservation of PSMalpha3 suggests a critical, potentially unknown, role for its amyloid-forming capacity.

Conclusions:

  • PSM amyloid formation appears to have limited relevance for established biological functions like cytolysis and biofilm stability.
  • PSM-DNA interactions provide a more plausible explanation for biofilm stabilization.
  • The stringent sequence requirements for PSMalpha3 amyloid formation hint at undiscovered functions crucial for staphylococcal biology.