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  11. The Secreted Staphylococcal Biofilm Protein Sbp Forms Biomolecular Condensates In The Presence Of Dna.
  1. Home
  3. Research Domains
  5. Biological Sciences
  7. Industrial Biotechnology
  9. Bioprocessing, Bioproduction And Bioproducts
  11. The Secreted Staphylococcal Biofilm Protein Sbp Forms Biomolecular Condensates In The Presence Of Dna.

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The secreted staphylococcal biofilm protein Sbp forms biomolecular condensates in the presence of DNA.

P Ethan Adkins1,2, Alexander E Yarawsky1, Andrew B Herr1,3,4

  • 1Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, USA.

Protein Science : a Publication of the Protein Society
|January 23, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Small basic protein (Sbp) from Staphylococcus epidermidis binds DNA, forming liquid-like droplets that transition to gels. This biomolecular condensation mechanism is crucial for organizing S. epidermidis biofilms, which cause device-related infections.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Staphylococcus epidermidis is a primary cause of device-related infections.
  • Biofilm formation by S. epidermidis confers resistance to antibiotics and host defenses.
  • Small basic protein (Sbp) is essential for S. epidermidis biofilm formation, but its function is poorly understood.

Purpose of the Study:

  • To investigate the function of S. epidermidis small basic protein (Sbp).
  • To elucidate the molecular mechanisms underlying Sbp's role in biofilm formation.
  • To determine if Sbp interacts with double-stranded DNA (dsDNA) and forms biomolecular condensates.

Main Methods:

  • In vitro DNA-binding assays were performed to assess Sbp-dsDNA interactions.
  • Confocal and differential interference contrast microscopy were used to visualize Sbp-dsDNA complexes.
Keywords:
Staphylococcus epidermidisaggregationanalytical ultracentrifugationbiofilmbiomolecular condensateconfocal microscopyextracellular DNAfluorescence recovery after photobleachingphase separationsmall basic protein

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  • Fluorescence recovery after photobleaching (FRAP) experiments were conducted to analyze the dynamics of Sbp-DNA condensates.

    • Main Results:

    • Sbp interacts with dsDNA, forming soluble complexes or aggregates depending on oligonucleotide length.
    • Sbp and dsDNA undergo phase separation to form droplets and/or solid aggregates.
    • Sbp-DNA condensate droplets exhibit liquid-like behavior that transitions to a gel-like state over time.

    Conclusions:

    • Sbp binds to dsDNA, a component of the biofilm matrix.
    • Sbp facilitates the formation of biomolecular condensates with dsDNA.
    • This Sbp-DNA condensation mechanism represents a novel pathway for S. epidermidis biofilm matrix organization.