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Porins of Pseudomonas fluorescens MFO as fibronectin-binding proteins
J Rebière-Huët1, J Guérillon, A L Pimenta
1Equipe de Recherche sur les Relations Matrice Extracellulaire-Cellules, UFR Sciences et Techniques St Martin, Université de Cergy-Pontoise, 2, avenue Adolphe Chauvin, P.O. Box 222, 95 302 Cedex, Cergy-Pontoise, France.
Abstract:
Bacterial adherence is a complex phenomenon involving specific interactions between receptors, including matricial fibronectin, and bacterial ligands. We show here that fibronectin and outer membrane proteins of Pseudomonas fluorescens were able to inhibit adherence of P. fluorescens to fibronectin-coated wells. We identified at least six fibronectin-binding proteins with molecular masses of 70, 55, 44, 37, 32 and 28 kDa. The presence of native (32 kDa) and heat-modified forms (37 kDa) of OprF was revealed by immuno-analysis and the 44-kDa band was composed of three proteins, their N-terminal sequences showing homologies with Pseudomonas aeruginosa porins (OprD, OprE1 and OprE3).
Insights
Pseudomonas fluorescens outer membrane proteins inhibit bacterial adherence to fibronectin. Researchers identified six fibronectin-binding proteins, including different forms of OprF and porin homologs, crucial for this interaction.
Area of Science:
- Microbiology
- Bacterial adhesion mechanisms
- Protein-ligand interactions
Background:
- Bacterial adherence is mediated by specific receptor-ligand interactions.
- Fibronectin serves as a key receptor for bacterial attachment.
Purpose of the Study:
- To investigate the role of Pseudomonas fluorescens outer membrane proteins in fibronectin binding.
- To identify specific fibronectin-binding proteins in P. fluorescens.
Main Methods:
- Inhibition assays using fibronectin-coated wells and P. fluorescens.
- Identification of bacterial proteins using molecular mass and N-terminal sequencing.
- Immuno-analysis to detect specific protein forms.
Main Results:
- Fibronectin and P. fluorescens outer membrane proteins inhibited bacterial adherence to fibronectin.
- Six fibronectin-binding proteins were identified (70, 55, 44, 37, 32, and 28 kDa).
- OprF (native 32 kDa, heat-modified 37 kDa) and three porin homologs (44 kDa band) were characterized.
Conclusions:
- Outer membrane proteins of P. fluorescens play a significant role in fibronectin adherence.
- Specific proteins, including OprF and porin homologs, are involved in fibronectin binding.