Listeria monocytogenes PdeE, a phosphodiesterase that contributes to virulence and has hydrolytic activity against cyclic mononucleotides and cyclic dinucleotides

- LMOf2365_2464 is a HD domain-containing hydrolase in Listeria monocytogenes.
- LMOf2365_2464 contributes to L. monocytogenes adherence and replication in host cells.
- LMOf2365_2464 contributes to L. monocytogenes colonization of mouse liver and spleen.
- The recombinant protein has strongest activity against cyclic di-AMP and cyclic AMP.
- Based on its activity, we designated LMOf2365_2464 phosphodiesterase E (PdeE).

We have identified and partially characterized a putative HD domain hydrolase, LMOf2365_2464, which is highly expressed during listerial intracellular replication. LMOf2365_2464 is annotated as a putative HD domain-containing hydrolase. The ability of an isogenic mutant strain, F2365Δ2464, to adhere, invade and replicate in intestinal epithelial cells (Caco-2) was significantly lower than parent strain F2365. Colonization of mouse liver and spleen by L. monocytogenes F2365 was significantly higher than it was for the mutant. The recombinant protein showed phosphodiesterase activity in the presence of divalent metal ions, indicating its role in nucleotide metabolism. It has activity against several cyclic nucleotides and cyclic dinucleotides, but its strongest activity is against cyclic di-AMP and cyclic AMP. Based on this enzymatic activity, we designated LMOf2365_2464 phosphodiesterase E (PdeE).