Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae

FEMS Microbiol Lett. 2000 Apr 1;185(1):17-22. doi: 10.1111/j.1574-6968.2000.tb09034.x.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial*
  • Animals
  • Bacterial Adhesion
  • Bacterial Proteins / antagonists & inhibitors
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / metabolism*
  • Chlorocebus aethiops
  • Endopeptidase K / metabolism
  • Fibronectins / metabolism
  • Humans
  • Leptospira interrogans / classification
  • Leptospira interrogans / metabolism
  • Leptospira interrogans / pathogenicity*
  • Receptors, Fibronectin / metabolism
  • Vero Cells
  • Virulence
  • Weil Disease / microbiology


  • Adhesins, Bacterial
  • Bacterial Proteins
  • Carrier Proteins
  • Fibronectins
  • Receptors, Fibronectin
  • fibronectin-binding proteins, bacterial
  • Endopeptidase K