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Binding of extracellular matrix proteins by enterococci

T W Zareba1, C Pascu, W Hryniewicz

  • 1Sera and Vaccines Central Research Laboratory, Chelmska str 30/34, PL 00-725 Warsaw, Poland.

Current Microbiology
|January 1, 1997
PubMed
Summary

Enterococcal strains bind human vitronectin, lactoferrin, and thrombospondin, with binding influenced by growth conditions and surface properties. Enterococcus faecalis strains showed higher hydrophobicity and protein binding than Enterococcus faecium.

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Enterococci are opportunistic pathogens frequently isolated from human clinical specimens.
  • Bacterial surface components play a crucial role in host-pathogen interactions, including adhesion to extracellular matrix (ECM) proteins.

Purpose of the Study:

  • To investigate the binding profiles of enterococcal strains to various human ECM proteins.
  • To explore the influence of growth conditions and surface characteristics on protein binding.
  • To identify potential mechanisms involved in enterococcal ECM protein interactions.

Main Methods:

  • Investigated binding of 125I-labeled fibronectin, vitronectin, thrombospondin, lactoferrin, collagen I, and collagen IV to 44 enterococcal strains.
  • Assessed cell surface hydrophobicity using particle agglutination assays (PAA).

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  • Examined the effects of heat, proteolytic digestion, and preincubation with unlabeled proteins or specific sugars/polymers on protein binding.

    • Main Results:

    • Most enterococcal strains exhibited higher binding to vitronectin, lactoferrin, and thrombospondin compared to fibronectin and collagens.
    • Growth in Todd-Hewitt broth enhanced binding to vitronectin and thrombospondin.
    • Enterococcus faecalis strains showed stronger PAA reactions and pronounced surface hydrophobicity than Enterococcus faecium strains.
    • Binding was affected by heating, proteolysis, and preincubation with specific sugars (galactose, fucose, mannosamine) and sulfated polymers, suggesting proteinaceous and potentially carbohydrate-mediated interactions.

    Conclusions:

    • Enterococci possess surface components that bind key ECM proteins, particularly vitronectin, lactoferrin, and thrombospondin.
    • Bacterial surface hydrophobicity and specific surface molecules influence ECM protein adherence.
    • These interactions may contribute to enterococcal colonization and pathogenesis in clinical settings.