Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae
| Autor: | Guy Baranton, Johann Truccolo, Philippe Perolat, Fabrice Merien |
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| Rok vydání: | 2000 |
| Předmět: |
Virulence
Microbiology Bacterial Adhesion Receptors Fibronectin Bacterial Proteins Leptospira Chlorocebus aethiops Genetics Animals Humans Adhesins Bacterial Molecular Biology Vero Cells biology biology.organism_classification Proteinase K Molecular biology Fibronectins Fibronectin Bacterial adhesin Fibronectin binding biology.protein Endopeptidase K Leptospira interrogans Weil Disease Carrier Proteins |
| Zdroj: | FEMS microbiology letters. 185(1) |
| ISSN: | 0378-1097 |
| Popis: | We investigated the ability of a virulent strain of Leptospira interrogans serovar icterohaemorrhagiae, its isogenic avirulent variant and a saprophytic strain to bind fibronectin using alkaline phosphatase-labelled fibronectin. A single 36-kDa fibronectin-binding protein was expressed only by the virulent strain and was located in the outer sheath according to proteinase K treatment results. The interaction of this protein with fibronectin was specific and the region of fibronectin bound to this potential adhesin overlapped the gelatin-binding domain. The inability of a RGDS synthetic peptide to inhibit the binding of fibronectin indicated that the cell-binding domain was not involved in this interaction. Considering the wide distribution of fibronectin within a host and the diversity of mammals involved in the epidemiology of leptospirosis, its implication in the cell attachment process of virulent leptospires is coherent with the multiplicity of target cells. |
| Databáze: | OpenAIRE |
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