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Fibronectin binding by Propionibacterium acnes

J L Yu1, R Månsson, J I Flock

  • 1Department of Medical Microbiology, University of Lund, Sweden.

FEMS Immunology and Medical Microbiology
|February 7, 1998
PubMed
Summary
This summary is machine-generated.

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Propionibacterium acnes, a common skin bacterium, can bind to fibronectin, a protein found in the body. Researchers identified an 80 kDa surface protein responsible for this binding, which may play a role in infections.

Area of Science:

  • Microbiology
  • Biochemistry
  • Infectious Diseases

Background:

  • Propionibacterium acnes (P. acnes) is implicated in various infections, including orthopaedic and biomaterial-associated ones.
  • Understanding bacterial adhesion mechanisms is crucial for developing effective treatments and preventative strategies.

Purpose of the Study:

  • To investigate the ability of P. acnes strains to bind fibronectin.
  • To identify potential fibronectin-binding proteins on the surface of P. acnes.

Main Methods:

  • Isolation and characterization of P. acnes strains from clinical samples and skin flora.
  • Fibronectin binding assays using immobilized and soluble fibronectin.
  • Protease and heat sensitivity assays.
  • SDS-PAGE and autoradiography to identify binding proteins.

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  • Inhibition assays using cell surface extracts and heparin.

    • Main Results:

    • Multiple P. acnes strains, particularly those from infections, demonstrated binding to immobilized fibronectin.
    • A specific 80 kDa surface protein was identified as the primary fibronectin-binding molecule.
    • Fibronectin binding was sensitive to protease and heat, and could be inhibited by heparin and cell surface extracts.

    Conclusions:

    • P. acnes possesses a surface-exposed 80 kDa protein that binds fibronectin.
    • This fibronectin-binding protein may contribute to the pathogenesis of P. acnes infections.
    • Further research into this protein could reveal new therapeutic targets.