期刊
MOLECULAR MICROBIOLOGY
卷 102, 期 2, 页码 336-348出版社
WILEY-BLACKWELL
DOI: 10.1111/mmi.13463
关键词
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资金
- National Institute of Allergy and Infectious Diseases (NIAID) [R01AI087946, R21AI113014]
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) [R01AR060834]
- Welch Foundation [AU-1714]
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.
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