title: Spirochetes flagellar collar protein FlbB has astounding effects in orientation of periplasmic flagella, bacterial shape, motility, and assembly of motors in Borrelia burgdorferi.
abstract: Borrelia burgdorferi, the causative agent of Lyme disease, is a highly motile spirochete, and motility, which is provided by its periplasmic flagella, is critical for every part of the spirochete's enzootic life cycle. Unlike externally flagellated bacteria, spirochetes possess a unique periplasmic flagellar structure called the collar. This spirochete-specific novel component is linked to the flagellar basal body; however, nothing is known about the proteins encoding the collar or their function in any spirochete. To identify a collar protein and determine its function, we employed a comprehensive strategy that included genetic, biochemical, and microscopic analyses. We found that BB0286 (FlbB) is a novel flagellar motor protein, which is located around the flagellar basal body. Deletion of bb0286 has a profound effect on collar formation, assembly of other flagellar structures, morphology, and motility of the spirochete. Orientation of the flagella toward the cell body is critical for determination of wild-type spirochete's wave-like morphology and motility. Here, we provide the first evidence that FlbB is a key determinant of normal orientation of the flagella and collar assembly.
authors.affiliation: Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
authors.forename: Ki Hwan
authors.initials: KH
authors.lastname: Moon
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA.
authors.forename: Xiaowei
authors.initials: X
authors.lastname: Zhao
authors.affiliation: Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
authors.forename: Akarsh
authors.initials: A
authors.lastname: Manne
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA.
authors.forename: Juyu
authors.initials: J
authors.lastname: Wang
authors.affiliation: Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
authors.forename: Zhou
authors.initials: Z
authors.lastname: Yu
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA. Jun.Liu.1@uth.tmc.edu.
authors.forename: Jun
authors.initials: J
authors.lastname: Liu
authors.affiliation: Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA. motalebm@ecu.edu.
authors.forename: Md A
authors.initials: MA
authors.lastname: Motaleb
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D025065:Borrelia burgdorferi / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D005407:Flagella / Q000235:genetics / Q000378:metabolism*; D020409:Molecular Motor Proteins / Q000235:genetics / Q000378:metabolism; D019897:Periplasm / Q000378:metabolism; D013144:Spirochaetales / Q000235:genetics / Q000378:metabolism; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D015534:Trans-Activators