Interactions de protéines de membrane externe de Pseudomonas aeruginosa avec la fibronectine plasmatique. Recherche d'adhésines bactériennes

Rebière-Huët, Julie; Martino, Patrick Di; Gallet, Olivier; Hulen, Christian

doi:10.1016/s0764-4469(99)00106-7

Cited by 12 publications

(7 citation statements)

References 43 publications

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“…These proteins corresponded to major OMPs. Several of these putative FnBPs show molecular masses similar to those previously observed for P. aeruginosa [12], and some of them could represent major porins. However, electrophoresis of OMPs in denaturing conditions could modify sufficiently their structure to let arise conformations that could be recognized by opsonin plasmatic Fn.…”

Section: Discussionsupporting

confidence: 73%

“…These results demonstrated that P. fluorescens has specific ligands for Fn. Since we previously demonstrated the OMPs involvement in P. aeruginosa specific adherence to Fn[12], we decided to investigate the existence of such FnBPs among OMPs of P. fluorescens MF0.…”

Section: Resultsmentioning

confidence: 99%

“…We had previously demonstrated that P. aeruginosa adheres to A549 pneumocyte cells, in part via their ECM fibronectin, and that several bacterial outer membrane proteins (OMPs) are specifically involved in the interaction with Fn [4,12,13]. This paper reports the involvement of porins from Pseudomonas fluorescens MF0 as fibronectin‐binding proteins (FnBPs).…”

Section: Introductionmentioning

confidence: 96%

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Porins ofPseudomonas fluorescensMFO as fibronectin-binding proteins

Rebière-Huët

Guerillon²,

Pimenta

et al. 2002

FEMS Microbiology Letters

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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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Section: Discussionsupporting

confidence: 73%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

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Porins ofPseudomonas fluorescensMFO as fibronectin-binding proteins

Rebière-Huët

Guerillon²,

Pimenta

et al. 2002

FEMS Microbiology Letters

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“…These results demonstrated that P. £uorescens has speci¢c ligands for Fn. Since we previously demonstrated the OMPs involvement in P. aeruginosa speci¢c adherence to Fn [12], we decided to investigate the existence of such FnBPs among OMPs of P. £uorescens MF0.…”

Section: Binding Of Pseudomonas £Uorescens To Immobilized ¢Bronectinmentioning

confidence: 99%

“…We had previously demonstrated that P. aeruginosa adheres to A549 pneumocyte cells, in part via their ECM ¢bronectin, and that several bacterial outer membrane proteins (OMPs) are speci¢cally involved in the interaction with Fn [4,12,13]. This paper reports the involvement of porins from Pseudomonas £uorescens MF0 as ¢bronectinbinding proteins (FnBPs).…”

Section: Introductionmentioning

confidence: 96%

Porins of Pseudomonas fluorescens MFO as fibronectin-binding proteins

Rebière-Huët¹

2002

FEMS Microbiology Letters

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Effects of Fibronectin Coating on Bacterial and Osteoblast Progenitor Cells Adherence in a Co-culture Assay

Hindié

Anselme

et al. 2016

Advances in Experimental Medicine and Biology

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Bacterial adherence to the surface of implants functionalized with cell-adhesive biomolecules is a critical first step of infection development. This study was designed to determine how the immobilization of human plasmatic fibronectin (pFN) could impact bacterial and osteoblast cells interaction with the surface during concomitant exposition to the two cell-types. Calibrated suspensions of P. aeruginosa PAOI or S. aureus CIP4.83 bacteria and STRO-1A osteoblast progenitor cells were mixed, co-seeded on glass coverslips coated or not with pFN and incubated at 37 °C. After 3 h of co-culture, the presence of bacteria did not modify the STRO-1A cells adherence to glass. pFN coating significantly enhanced STRO-1A cells, CIP4.83 and PAOI adherence to glass and bacterial interaction with STRO-1A cells. Confocal laser scanning microscopy observations revealed that cells on the pFN-coated substrate exhibited a greater spreading, better organized network of cytoskeletal filaments, and an increased cellular FN expression than cells on the uncoated substrate. The use of fluorescently labeled pFN showed that adherent STRO-1A cells were able to remodel and to concentrate coated pFN at the cells surface. Thus, the use of FN coating could increase the risk of bacterial adherence to the material surface, acting either directly onto the coating layer or indirectly on adherent osteoblastic cells. This may increase the infection risk in the presence of bacterial contamination.

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Interactions de protéines de membrane externe de Pseudomonas aeruginosa avec la fibronectine plasmatique. Recherche d'adhésines bactériennes

Cited by 12 publications

References 43 publications

Porins ofPseudomonas fluorescensMFO as fibronectin-binding proteins

Porins ofPseudomonas fluorescensMFO as fibronectin-binding proteins

Porins of Pseudomonas fluorescens MFO as fibronectin-binding proteins

Effects of Fibronectin Coating on Bacterial and Osteoblast Progenitor Cells Adherence in a Co-culture Assay

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