Speakers
Description
Bacterial flagella are remarkable, highly sophisticated organelles primarily evolved for motility. These complex structures are composed of thousands of protein subunits, specifically flagellin, arranged in a helical filament. Intrigued by our discovery that several bacterial species naturally possess proteolytic domains on their flagellar surface, effectively transforming their flagella into massive proteolytic machineries, we are employing synthetic microbiology and structural protein engineering to systematically repurpose these ubiquitous bacterial appendages.
Our overarching goal is to augment structural flagellins with a diverse range of novel enzymatic or binding functions, creating programmable cellular nanomachines capable of performing specific tasks. To achieve this, we rely on a robust integrative structural biology pipeline. By combining high-resolution macromolecular crystallography (MX) of individual functional domains—utilizing ALBA’s XALOC and XAIRA beamlines—with single-particle cryo-electron microscopy (JEMCA) of the assembled filaments, we can precisely control the display of these engineered functionalities.
We are currently focusing our efforts on expanding this platform to explore novel bacterial surface modifications and optimize the efficiency of our engineered systems. Looking toward the enhanced multimodal imaging capabilities of ALBA II, we plan to leverage soft X-ray cryo-tomography (MISTRAL) to investigate our engineered cellular nanomachines in situ. This will allow us to visualize their spatial distribution, assembly states, and host-target interactions directly within their native cellular environment. Our long-term vision is to develop a versatile, structurally-guided platform for creating custom-designed bacteria for targeted biotechnological and biomedical applications.