Md A. Motaleb

This study reveals how asymmetric FlaA sheath assembly in Borreliella burgdorferi flagella influences morphology and motility through structural and genetic analyses.

The paper identifies a molecular clutch mechanism in Borrelia burgdorferi flagellar motors that controls stator engagement and torque generation through distinct conformational states.

This study uses in situ cryo-EM to reveal how the flagellar motor in Borrelia burgdorferi transmits high torque through mechanical coupling and a split washer-shaped FrbA brace.

This paper identifies FlcE as a flagellar collar protein in Borrelia burgdorferi that stabilizes the FliL-stator complex, enhancing motility and torque generation.

This study uses cryo-EM to determine the structure of the flagellar export apparatus in Borrelia burgdorferi, revealing its assembly mechanism and role in substrate translocation.

The paper uses cryo-electron tomography to study the flagellar motor in Borrelia burgdorferi, revealing conformational changes in the C-ring essential for flagellar rotation.

The paper uses cryo-electron tomography and mutagenesis to study the fT3SS machine in Borrelia burgdorferi, revealing a distinct cytosolic ATPase complex linked to the flagellar C-ring.