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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 : Molecular microbiology

A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 26 Apr 2016

Wunder EA, Figueira CP, Benaroudj N, Hu B, Tong BA, Trajtenberg F, Liu J, Reis MG, Charon NW, Buschiazzo A, Picardeau M, Ko AI

Link to Pubmed [PMID] – 27113476

Mol. Microbiol. 2016 Apr;

Leptospira are unique among bacteria based on their helical cell morphology with hook-shaped ends and the presence of periplasmic flagella (PF) with pronounced spontaneous supercoiling. The factors that provoke such supercoiling, as well as the role that PF coiling plays in generating the characteristic hook-end cell morphology and motility, have not been elucidated. We have now identified an abundant protein from the pathogen L. interrogans, exposed on the PF surface, and named it Flagellar-coiling protein A (FcpA). The gene encoding FcpA is highly conserved among Leptospira and was not found in other bacteria. fcpA(-) mutants, obtained from clinical isolates or by allelic exchange, had relatively straight, smaller-diameter PF, and were not able to produce translational motility. These mutants lost their ability to cause disease in the standard hamster model of leptospirosis. Complementation of fcpA restored the wild-type morphology, motility and virulence phenotypes. In summary, we identified a novel Leptospira 36-kDa protein, the main component of the spirochete’s PF sheath, and a key determinant of the flagella’s coiled structure. FcpA is essential for bacterial translational motility and to enable the spirochete to penetrate the host, traverse tissue barriers, disseminate to cause systemic infection, and reach target organs. This article is protected by copyright. All rights reserved.

http://www.ncbi.nlm.nih.gov/pubmed/27113476