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© Institut Pasteur
Spirochète : bactérie hélicoïdale, flexible et ondulante de longueur variable, non colorable par la coloration de Gram, très mobile (endoflagelles). Trois familles : Spirochaetaceae, Leptospiraceae, et Brachyspiraceae. Principaux genres pathogènes pour l'homme : Borrelia (Borrelia burgdorferi cause de la maladie de Lyme), Treponema (Treponema pallidum cause de la syphillis), Leptospira (Leptospira interrogans serovar icterohaemorrhagiae cause de la maladie de Weil). Image colorisée.
Publication : Acta crystallographica. Section D, Biological crystallography

Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Biological crystallography - 23 May 2015

Miras I, Saul F, Nowakowski M, Weber P, Haouz A, Shepard W, Picardeau M

Link to Pubmed [PMID] – 26057675

Acta Crystallogr. D Biol. Crystallogr. 2015 Jun;71(Pt 6):1351-9

Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic α/β-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria.

http://www.ncbi.nlm.nih.gov/pubmed/26057675