Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/15272
Title: A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete
Authors: Wunder Júnior, Elsio Augusto
Figueira, Cláudio Pereira
Benaroudj, Nadia
Hu, Bo
Tong, Brian A
Trajtenberg, Felipe
Liu, Jun
Reis, Mitermayer Galvão dos
Charon, Nyles W
Buschiazzo, Alejandro
Picardeau, Mathieu
Ko, Albert Icksang
Affilliation: Yale School of Public Health. Department of Epidemiology of Microbial Disease. New Haven, Connecticut, USA / Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Institut Pasteur. Unit of Biology of Spirochetes. Paris, France
University of Texas Medical School at Houston. Department of Pathology and Laboratory Medicine. Houston, USA
University of Texas Medical School at Houston. Department of Pathology and Laboratory Medicine. Houston, USA
Institut Pasteur de Montevideo. Laboratory of Molecular & Structural Microbiology. Montevideo, Uruguay
University of Texas Medical School at Houston. Department of Pathology and Laboratory Medicine. Houston, USA
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
West Virginia University. Department of Microbiology and ImmunologyMorgantown. WV, USA
University of Texas Medical School at Houston. Department of Pathology and Laboratory Medicine. Houston, USA / Institute Pasteur. Department of Structural Biology and Chemistry. Paris, France.
Institut Pasteur. Unit of Biology of Spirochetes. Paris, France
Yale School of Public Health. Department of Epidemiology of Microbial Disease. New Haven, Connecticut, USA / Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Abstract: 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.
Keywords: Leptospira
Leptospirosis
Spirochete
Virulence
Flagella
Phenotypes
Animals
Cricetinae
Issue Date: 2016
Publisher: Wiley
Citation: WUNDER JÚNIOR, E. A. et al. A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete. Molecular Microbiology, 2016.
DOI: 10.1111/mmi.13403
ISSN: 0950-382X
Copyright: open access
Appears in Collections:BA - IGM - Artigos de Periódicos

Files in This Item:
File Description SizeFormat 
Wunder Jr EA A novel flagellar....pdf1.27 MBAdobe PDFView/Open


FacebookTwitterDeliciousLinkedInGoogle BookmarksBibTex Format mendeley Endnote DiggMySpace

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.