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Journal of Bacteriology, August 2009, p. 5026-5036, Vol. 191, No. 16
0021-9193/09/$08.00+0     doi:10.1128/JB.00340-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Intact Flagellar Motor of Borrelia burgdorferi Revealed by Cryo-Electron Tomography: Evidence for Stator Ring Curvature and Rotor/C-Ring Assembly Flexion{triangledown} ,{dagger}

Jun Liu,1* Tao Lin,1 Douglas J. Botkin,1,2 Erin McCrum,1 Hanspeter Winkler,3 and Steven J. Norris1,2

Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, Houston, Texas 77030,1 Department of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas 77030,2 Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 323063

Received 11 March 2009/ Accepted 1 May 2009

The bacterial flagellar motor is a remarkable nanomachine that provides motility through flagellar rotation. Prior structural studies have revealed the stunning complexity of the purified rotor and C-ring assemblies from flagellar motors. In this study, we used high-throughput cryo-electron tomography and image analysis of intact Borrelia burgdorferi to produce a three-dimensional (3-D) model of the in situ flagellar motor without imposing rotational symmetry. Structural details of B. burgdorferi, including a layer of outer surface proteins, were clearly visible in the resulting 3-D reconstructions. By averaging the 3-D images of ~1,280 flagellar motors, a ~3.5-nm-resolution model of the stator and rotor structures was obtained. flgI transposon mutants lacked a torus-shaped structure attached to the flagellar rod, establishing the structural location of the spirochetal P ring. Treatment of intact organisms with the nonionic detergent NP-40 resulted in dissolution of the outermost portion of the motor structure and the C ring, providing insight into the in situ arrangement of the stator and rotor structures. Structural elements associated with the stator followed the curvature of the cytoplasmic membrane. The rotor and the C ring also exhibited angular flexion, resulting in a slight narrowing of both structures in the direction perpendicular to the cell axis. These results indicate an inherent flexibility in the rotor-stator interaction. The FliG switching and energizing component likely provides much of the flexibility needed to maintain the interaction between the curved stator and the relatively symmetrical rotor/C-ring assembly during flagellar rotation.

* Corresponding author. Mailing address: Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin, MSB 2.228, Houston, TX 77030. Phone: (713) 500-5342. Fax: (713) 500-0730. E-mail: jun.liu.1{at}uth.tmc.edu

{triangledown} Published ahead of print on 8 May 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, August 2009, p. 5026-5036, Vol. 191, No. 16
0021-9193/09/$08.00+0     doi:10.1128/JB.00340-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

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Michael D. Manson and Mark L. Harlow
JB 2009 191: 5023-5025. [Full Text]  



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