Journal
PLOS BIOLOGY
Volume 16, Issue 11, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.3000050
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Funding
- National Institute of Allergy and Infectious Diseases [R01AI087946, R01AI078958, R01AI132818, 1R01AI59048]
- National Institute of Dental and Craniofacial Research [R01DE023080]
- Welch Foundation [AU1714]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI087946, R01AI132818, R01AI059048, R01AI078958] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH [R01DE023080] Funding Source: NIH RePORTER
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Periplasmic flagella are essential for the distinct morphology and motility of spirochetes. A flagella-specific type III secretion system (fT3SS) composed of a membrane-bound export apparatus and a cytosolic ATPase complex is responsible for the assembly of the periplasmic flagella. Here, we deployed cryo-electron tomography (cryo-ET) to visualize the fT3SS machine in the Lyme disease spirochete Borrelia burgdorferi. We show, for the first time, that the cytosolic ATPase complex is attached to the flagellar C-ring through multiple spokes to form the spoke and hub structure in B. burgdorferi. This structure not only strengthens structural rigidity of the round-shaped C-ring but also appears to rotate with the C-ring. Our studies provide structural insights into the unique mechanisms underlying assembly and rotation of the periplasmic flagella and may provide the basis for the development of novel therapeutic strategies against several pathogenic spirochetes.
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