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05:57
In Vitro Assay of Bacterial Adhesion onto Mammalian Epithelial Cells
Published on: May 16, 2011
Adherence of Pasteurella multocida to fibronectin
S M Dabo1, A W Confer, S D Hartson
1Department of Veterinary Pathobiology, Oklahoma State University, Stillwater, OK 74078-2007, USA. mady.dabo@okstate.edu
Veterinary Microbiology
|September 20, 2005
Summary
Pasteurella multocida binds to host fibronectin (Fn) via surface proteins, particularly the N-terminal Hep-binding domain. This interaction is crucial for bacterial adherence to host cells, with potential implications for pathogenesis.
Area of Science:
- Microbiology
- Molecular Biology
- Pathogenesis
Background:
- Pathogen adherence to host extracellular matrix (ECM) is vital for infection.
- Fibronectin (Fn) is a key ECM component involved in pathogen-host interactions.
Purpose of the Study:
- To investigate the interaction between Pasteurella multocida and fibronectin (Fn).
- To identify bacterial components and Fn domains involved in adherence.
Main Methods:
- Bacterial binding assays with Fn and collagen types.
- Inhibition studies using heparin (Hep) and anti-Fn antibodies.
- Protease treatment, ligand blotting, affinity purification, and mass spectrometry (MALDI-TOF).
Main Results:
- P. multocida significantly binds Fn and collagen IX, but not laminin or collagen IV/X.
- Binding to Fn is dose-dependent, inhibited by Hep, and enhanced by capsule removal.
- Surface proteins mediate binding to the N-terminal Hep-binding domain of Fn.
- Fn and anti-Fn antibodies inhibit bacterial adherence to host cells.
Conclusions:
- P. multocida utilizes surface proteins to bind the N-terminal Hep-binding domain of fibronectin.
- This interaction is critical for P. multocida adherence to host cells.
- Fn-mediated adherence is a potential virulence mechanism for P. multocida.
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