Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex.
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Date
2018-11-09
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Authors
Qin, Zhuan
Tu, Jiagang
Lin, Tao
Norris, Steven J.
Li, Chunhao
Motaleb, Md A.
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Abstract
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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DOI
10.1371/journal.pbio.3000050