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Fibronectin-binding activity in Borrelia burgdorferi1
D J Grab1, C Givens, R Kennedy
1Department of Parasitology, Tulane Regional Primate Research Center, Covington, LA, USA. grab@cc.saga-u.ac.jp
Biochimica Et Biophysica Acta
|August 1, 1998
Summary
Borrelia burgdorferi and related species possess surface molecules that bind to fibronectin, a component of the host extracellular matrix. These fibronectin-binding proteins (Fn-BAs) may facilitate spirochete adhesion and interaction with host tissues.
Area of Science:
- Microbiology
- Molecular Biology
- Immunology
Background:
- Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) are key to pathogen-host interactions.
- The extracellular matrix (ECM) plays a crucial role in cellular structure and communication.
- Understanding pathogen adhesion mechanisms is vital for developing effective treatments.
Purpose of the Study:
- To investigate the presence and characteristics of fibronectin-binding molecules on Borrelia burgdorferi and other Borrelia species.
- To determine the role of these molecules in the interaction between Borrelia and the host extracellular matrix.
Main Methods:
- Immunofluorescence microscopy to visualize fibronectin binding on B. burgdorferi.
- Microtiter plate assays to quantify spirochete binding to fibronectin.
- Western blot-like assays to identify and characterize fibronectin-binding proteins (Fn-BAs).
Main Results:
- Plasma fibronectin uniformly binds to the surface of B. burgdorferi.
- Borrelia species demonstrate significant binding to fibronectin, which can be inhibited by anti-fibronectin antibodies and excess fibronectin.
- B. burgdorferi and B. afzelii express a major 52 kDa Fn-BA, while other Borrelia species exhibit multiple Fn-BAs of varying molecular masses.
Conclusions:
- Borrelia species possess surface molecules that bind to host fibronectin.
- Fibronectin-binding proteins (Fn-BAs) on Borrelia spirochetes are identified.
- Fn-BAs likely act as molecular bridges, mediating the interaction between spirochetes and the extracellular matrix, potentially contributing to pathogenesis.