Recombinant csgC protein

The CsgC protein is a key component of the curli fibrils produced by *Escherichia coli* and other Enterobacteriaceae. Curli are functional amyloid fibers critical for bacterial biofilm formation, host cell adhesion, and immune evasion, contributing to bacterial persistence and pathogenicity. The *csg* operon encodes structural (CsgA, CsgB) and regulatory/assembly proteins (CsgC, CsgE, CsgF, CsgG). CsgC, specifically, acts as a chaperone-like protein essential for curli biogenesis. It interacts with the major curli subunit CsgA, preventing premature aggregation in the bacterial periplasm and facilitating proper fibril assembly on the cell surface.

Recombinant CsgC is engineered for studies on amyloid formation mechanisms and bacterial pathogenesis. Its production typically involves cloning the *csgC* gene into expression vectors (e.g., pET systems) followed by purification via affinity chromatography. Research highlights its role in modulating amyloidogenicity, with potential applications in understanding neurodegenerative diseases linked to amyloid misfolding, such as Alzheimer’s. Additionally, recombinant CsgC serves as a tool for developing anti-biofilm strategies, as disrupting curli assembly could mitigate bacterial virulence. Recent studies also explore its use in bio-nanotechnology due to its ability to stabilize and template nanostructures. Despite its structural simplicity, CsgC's dual role in pathogenicity and amyloid regulation makes it a compelling target for therapeutic and biotechnological innovation. Ongoing research aims to unravel its precise molecular interactions and exploit its properties for antimicrobial or material science applications.