Flagellar assembly and motility proteins (Helicobacter pylori)

Helicobacter pylori is a Gram-negative bacterium that colonizes the human stomach, leading to chronic gastritis, peptic ulcers, and gastric cancer (Lertsethtakarn et al., 2011). Its ability to survive and colonize the harsh, acidic gastric environment is strictly dependent on its flagellar system, which provides the motility required to penetrate the thick gastric mucus layer (Tsang & Hoover, 2014). The flagellar assembly and motility proteins form a complex, multi-component machine consisting of a basal body, a hook, and a filament composed primarily of FlaA and FlaB flagellins (UniProt P0A0S1). This machinery is powered by a proton-driven motor (MotA/MotB) and regulated by a chemotaxis system that directs the bacteria toward the epithelial surface. Because motility is a prerequisite for virulence and persistent infection, these proteins are considered high-priority therapeutic targets for the development of non-antibiotic or narrow-spectrum antimicrobial strategies. Experimental inhibitors targeting the FliI ATPase or the motor proteins have shown promise in reducing bacterial load and preventing colonization in animal models (Machuca et al., 2017). Targeting this system offers a way to specifically combat H. pylori while potentially minimizing the impact on the broader gut microbiota compared to traditional broad-spectrum antibiotics.

Other names

Flagellar apparatusFlagellar motor complexFlagellar biosynthetic pathwayH. pylori motility systemFlagellar regulon

Inhibition of flagellar assembly, disruption of the proton-driven motor function, or inhibition of the FliI ATPase to prevent bacterial motility and colonization.