Porins of Pseudomonas fluorescens MFO as fibronectin-binding proteins
J Rebiere-Huet, J Guérillon, AL Pimenta… - FEMS microbiology …, 2002 - academic.oup.com
J Rebiere-Huet, J Guérillon, AL Pimenta, P Di Martino, N Orange, C Hulen
FEMS microbiology letters, 2002•academic.oup.comBacterial 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 …
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 …
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).
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