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Flagellar hook protein FlgE is a critical structural component of the bacterial flagellum, functioning as the primary subunit of the flagellar hook. This hook serves as a molecular universal joint that transmits rotational torque from the motor (basal body) to the propeller-like filament, which is essential for bacterial motility and chemotaxis. Beyond its mechanical function, FlgE acts as a significant virulence factor by facilitating host cell adhesion, tissue invasion, and the development of antibiotic-tolerant biofilms. Recent studies have identified FlgE as a pro-inflammatory agent that interacts with host cell receptors such as caveolin-1 and ectopic ATP synthase subunit beta (ATP5B), leading to the induction of cytokines and vascular hyperpermeability. Due to its essential role in virulence and its accessibility on the bacterial surface, FlgE is being investigated as a target for anti-virulence drugs and as a protective antigen in vaccine development against pathogens like Pseudomonas aeruginosa and Borrelia burgdorferi.
Inhibition of flagellar hook assembly, Opsonophagocytic killing (via antibodies), Neutralization of bacterial motility, Blocking of host-cell receptor binding
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