2002
DOI: 10.1016/s0378-1097(02)00920-5
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Porins of Pseudomonas fluorescens MFO as fibronectin-binding proteins

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 … Show more

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Cited by 29 publications
(13 citation statements)
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“…Using two cellular models, we show here that the decreased toxicity of the oprF mutant is at least partially due to its lowered ability to adhere to cells. This confirms the role of OprF as a cellular adhesin, as previously described using lung epithelial cells (2), fibronectin (58), and wheat root cells, in the case of Pseudomonas fluorescens OE28.3 (20). Furthermore, the reduction of the oprF mutant toxicity is unlikely ascribed only to a lessened affinity to target cells, since a strong decrease was also observed (i) in the production of the exoproducts, namely, pyocyanin, lectin PA-1L, exotoxin A, and elastase, which have cytotoxic properties contributing to tissue damage and to the pathogenesis of P. aeruginosa (36,41,61,77), and (ii) in the activity of T3SS.…”
Section: Discussionsupporting
confidence: 90%
“…Using two cellular models, we show here that the decreased toxicity of the oprF mutant is at least partially due to its lowered ability to adhere to cells. This confirms the role of OprF as a cellular adhesin, as previously described using lung epithelial cells (2), fibronectin (58), and wheat root cells, in the case of Pseudomonas fluorescens OE28.3 (20). Furthermore, the reduction of the oprF mutant toxicity is unlikely ascribed only to a lessened affinity to target cells, since a strong decrease was also observed (i) in the production of the exoproducts, namely, pyocyanin, lectin PA-1L, exotoxin A, and elastase, which have cytotoxic properties contributing to tissue damage and to the pathogenesis of P. aeruginosa (36,41,61,77), and (ii) in the activity of T3SS.…”
Section: Discussionsupporting
confidence: 90%
“…As reported for recent proteomic studies, the OprD homologue, which is overexpressed during sessile growth mode, would promote A. baumannii biofilm formation (8,35). It is tempting to consider that this protein might be involved in cell adhesion, as its OprQ counterparts are in P. aeruginosa and P. fluorescens binding to fibronectin (2,49). Associated with its particular affinity for iron, these features could contribute to the involvement of the OprD homologue (which could now be called the OprQ-like protein) in the host colonization process and make it a potential and important virulence factor of A baumannii.…”
Section: Resultsmentioning
confidence: 92%
“…Fibronectin were pre-coated in sterile 96-well sterile plates as described previously [14]. Briefly, 100 μL fibronectin (Sigma-Aldrich, St. Louis, USA) at 0.1 mg/mL concentration was added to each well overnight, while 20 mg/mL bovine serum albumin (BSA) was added to three wells as blank control wells.…”
Section: Biofilm Production Assaymentioning
confidence: 99%