Type III secretion system ATPase (SctN)

The Type III secretion system (T3SS) ATPase is a highly conserved enzyme essential for the virulence of many Gram-negative pathogens, including Salmonella, Shigella, and Pseudomonas [1.4.3]. It belongs to the AAA+ family of ATPases and provides the energy required for the unfolding and translocation of effector proteins through the needle-like injectisome into host cells [1.3.5, 1.4.3]. In the flagellar system, the homologous ATPase (FliI) drives the export of flagellar subunits necessary for bacterial motility [1.2.1, 1.4.1]. Because these ATPases are critical for pathogenesis but not for bacterial survival under standard conditions, they are attractive targets for anti-virulence therapies that neutralize pathogens without exerting the strong selective pressure associated with traditional antibiotics [1.3.1, 1.3.5]. Small molecule inhibitors, such as salicylidene acylhydrazides and novel non-competitive inhibitors, have shown promise in blocking ATPase activity and reducing the secretion of virulence factors in various infection models [1.3.3, 1.3.5]. Targeting this enzyme offers a strategy to treat infections while potentially reducing the development of antibiotic resistance [1.3.1].

Other names

FliIEscNSpa47InvCYscNHrpB6VscNBsaSHrcNFlagellar export ATPaseType III secretion system protein N

Inhibition of ATP hydrolysis and energy coupling to the T3SS export gate, preventing the secretion of virulence effector proteins [1.3.1, 1.3.3].