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Conditional adherence of Enterococcus faecalis to extracellular matrix proteins

J Xiao1, M Höök, G M Weinstock

  • 1Center for the Study of Emerging and Re-emerging Pathogens, Department of Internal Medicine, University of Texas Medical School, Houston 77030, USA.

FEMS Immunology and Medical Microbiology
|September 30, 1998
PubMed
Summary

Enterococcus faecalis adherence to extracellular matrix proteins varies with growth conditions. Stressful temperatures like 46°C can increase adherence in E. faecalis, but not E. faecium, suggesting a role in potential infections.

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Biochemistry

Background:

  • Enterococcus faecalis is a significant cause of endocarditis.
  • Bacterial adherence to host extracellular matrix (ECM) proteins is crucial for infection development.
  • Understanding adherence mechanisms can inform strategies to combat enterococcal infections.

Purpose of the Study:

  • To investigate the adherence of clinical isolates of Enterococcus faecalis and Enterococcus faecium to various ECM proteins.
  • To determine the influence of different in vitro growth conditions on bacterial adherence.
  • To identify potential bacterial factors involved in ECM adherence.

Main Methods:

  • Utilized 35S-labeled bacteria to quantify adherence of 44 E. faecalis and 13 E. faecium isolates to six ECM proteins.

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  • Assessed adherence under standard growth conditions (37°C) and under stress conditions (46°C, CO2 enrichment, nutrient limitation).
  • Investigated the role of proteins in adherence using trypsin digestion and assessed the effect of pre-incubation with soluble ECM proteins.

    • Main Results:

    • Most isolates showed minimal adherence at 37°C, irrespective of the source.
    • Elevated temperature (46°C) significantly increased E. faecalis adherence to laminin and collagen types I and IV, but not fibronectin, fibrinogen, or BSA.
    • E. faecium isolates did not show increased adherence at elevated temperatures (46°C or 50°C).
    • Trypsin digestion eliminated E. faecalis adherence, indicating protein involvement.
    • Pre-incubation with soluble collagen inhibited bacterial adherence to collagen substrates.

    Conclusions:

    • Enterococcus faecalis exhibits temperature-dependent adherence to specific ECM proteins, suggesting a role for stress conditions in promoting adherence.
    • Adherence is mediated by proteins, potentially involving direct interaction with ECM components like collagen.
    • The variable adherence patterns observed highlight the adaptability of E. faecalis and warrant further investigation into its link with endocarditis pathogenesis.