Identification of a fibronectin-binding protein of Treponema lecithinolyticum by two-dimensional gel electrophoresis and ligand binding assay

Can J Microbiol. 2007 Oct;53(10):1185-90. doi: 10.1139/W07-086.

Abstract

Treponema lecithinolyticum is associated with periodontitis and endodontic infections. As a critical early step in the infection process, fibronectin-binding protein (Fbp) is known to be involved in the adhesion of bacteria to cell surfaces for colonization and, hence, is considered to be a virulence factor. In this study, we identified an Fbp from the T. lecithinolyticum cell surface with a molecular mass of about 52 kDa by using 2-dimensional gel electrophoresis followed by a ligand binding assay. As T. lecithinolyticum is capable of binding to soluble and immobilized fibronectin, this Fbp may contribute to bacterial attachment to host cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Fibronectins / metabolism*
  • Humans
  • Ligands
  • Molecular Sequence Data
  • Protein Binding
  • Treponema / metabolism*

Substances

  • Bacterial Proteins
  • Fibronectins
  • Ligands