Bergeron lab
@ the University of Sheffield

Structure and mechanism of macromolecular nano-machines

Structural characterization of the bacterial flagellum

The bacterial flagellum is an appendage whose primary role is to allow bacterial motility. It is also a key component in the formation of bacterial biofilms, a major factor in the establishment of antibiotic resistance. Finally, the flagellum has  numerous potential nanotechnology applications, and could be used for the design of small propelled devices, such as drug-delivery vesicles.

The flagellum consists of an export apparatus localized in the cytoplasmic side of the inner-membrane, which allows assembly and rotation of the system; a basal body, spanning both membranes and the periplasmic space; and the hook-filament structure that protrudes away from the bacterium. Importantly, although the flagellum and T3SS perform different functions, they are evolutionarily related, with a number of homologous components. Nonetheless, many flagellum proteins, including most of the basal body, the hook and the filament, do not show any detectable homology with T3SS proteins. I am mostly interested in characterizing these regions, using a combination of structural, biochemical and cell-based assays.

Related publications:

Bergeron JRC. Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex. PeerJ 2016.

Latest News

22/12/16 - The cryo-EM structure of the T3SS basal body has been published in the journal Nature:

02/12/16 - I am recruiting a PhD student to join my (forthcoming) lab in the Department of Molecular Biology and Biotechnology at the University of Sheffield, UK. Interested candidates should apply here.

30/10/16 - I will be giving a talk at the Sheffield Imagine: Imaging Life launch symposium, in January 2017: