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Related Experiment Videos

Ace is a collagen-binding MSCRAMM from Enterococcus faecalis.

R L Rich1, B Kreikemeyer, R T Owens

  • 1Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|September 10, 1999
PubMed
Summary
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Enterococcus faecalis possesses a novel collagen-binding protein, Ace, structurally similar to Staphylococcus aureus Cna. This protein mediates bacterial adhesion to collagen, highlighting its role in enterococcal infections.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-positive bacteria utilize MSCRAMM proteins for adherence.
  • Staphylococcus aureus Cna protein is a well-characterized collagen-binding MSCRAMM.
  • Enterococcus faecalis adhesion mechanisms are not fully understood.

Purpose of the Study:

  • To identify and characterize a collagen-binding MSCRAMM in Enterococcus faecalis.
  • To investigate the structural and functional relationship between the novel protein and S. aureus Cna.
  • To assess the role of the identified protein in enterococcal collagen binding.

Main Methods:

  • Bioinformatic analysis of bacterial genome databases.
  • Protein expression and purification of recombinant Ace A domain.

Related Experiment Videos

  • Antibody generation and functional inhibition assays.
  • Structural modeling and CD spectroscopy.
  • Biochemical analysis of protein-collagen interactions.
  • Main Results:

    • A putative collagen-binding MSCRAMM, Ace, was identified in E. faecalis.
    • Ace shares significant sequence homology and structural similarity with S. aureus Cna.
    • Antibodies against Ace inhibited E. faecalis adhesion to collagen.
    • Ace binds type I collagen with micromolar affinity.

    Conclusions:

    • Ace is a functional collagen-binding MSCRAMM in E. faecalis.
    • Ace is structurally and functionally related to the S. aureus Cna protein.
    • Ace likely plays a significant role in enterococcal colonization and pathogenesis.