Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex.

ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)

Zhuan,Tu,Jiagang,Lin,Tao,Norris,Steven J.,Li,Chunhao,Motaleb,Md A. Qin (Creator)

Institution

East Carolina University (ECU )

Web Site: http://www.ecu.edu/lib/

Abstract: Periplasmic flagella are essential for the distinct morphology and motility of spirochetes. Aflagella-specific type III secretion system (fT3SS) composed of a membrane-bound exportapparatus 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 fT3SSmachine 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 spokesto form the "spoke and hub" structure in B. burgdorferi. This structure not only strengthensstructural rigidity of the round-shaped C-ring but also appears to rotate with the C-ring. Ourstudies provide structural insights into the unique mechanisms underlying assembly androtation of the periplasmic flagella and may provide the basis for the development of noveltherapeutic strategies against several pathogenic spirochetes.

Additional Information

Publication

Other

Language: English

Date: 2018

Email this document to