Abstract 2398 Actin-activated ATP to AMP conversion by an effector from the pathogen Legionella pneumophila

Bacterial pathogens secrete protein toxins and effectors that hijack metabolites such as nicotinamide adenine dinucleotide (NAD+) and adenosine triphosphate (ATP) to post-translationally modify host proteins and reprogram host pathways that interfere with their function during infection. AMPylation, the covalent addition of AMP moiety to target substrates, is one such regulatory mechanism playing significant roles in both prokaryotic and eukaryotic biology.Recently, we (and others) described an actin-dependent AMPylase called LnaB from the bacterial pathogen Legionella pneumophila which was found to AMPylate phosphate groups of phospho-ribosylated ubiquitin (PR-Ub) and phospho-tyrosine residues of Src family kinases.