Legionella effector protein Ceg14 (Ceg14)

Ceg14, also known as SidL, is a potent effector protein secreted by the opportunistic human pathogen Legionella pneumophila through its Dot/Icm type IV secretion system [1, 7]. It plays a critical role in host-pathogen interactions by acting as an actin-activated ATPase and dATPase, which catalyzes the conversion of cellular ATP and dATP into adenosine and deoxyadenosine monophosphate [2, 9]. This enzymatic activity, stimulated by binding to host actin, leads to the depletion of cellular energy stores and the direct inhibition of actin polymerization, resulting in significant disruption of the host cytoskeleton and suppression of mRNA translation [1, 4, 13]. Such activities are essential for the bacterium to establish a specialized replicative niche, the Legionella-containing vacuole (LCV), and to evade the host's innate immune response [8, 13]. While currently a subject of fundamental research rather than a target for approved pharmaceuticals, Ceg14 is endogenously regulated by the bacterial metaeffector AnkJ (LegA11) and its toxicity can be suppressed by host profilin, making it a key molecular target for understanding bacterial virulence mechanisms and potential antivirulence drug development [3, 4, 6].

Other names

SidLLpg0437LPG_RS02190Dot/Icm T4SS effector Ceg14

None currently known; Ceg14 is a potential target for experimental antivirulence inhibitors to prevent host cytoskeleton disruption and ATP depletion during infection.