Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA

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Kandiah, Eaazhisai | Carriel, Diego | Garcia, Pierre Simon | Felix, Jan | Banzhaf, Manuel | Kritikos, George | Bacia-Verloop, Maria | Brochier-Armanet, Céline | Elsen, Sylvie | Gutsche, Irina

Edité par CCSD ; Elsevier (Cell Press) -

International audience. The only enzyme responsible for cadaverine production in the major multidrug-resistant human pathogen Pseudomonas aeruginosa is the lysine decarboxylase LdcA. This enzyme modulates the general polyamine homeostasis, promotes growth, and reduces bacterial persistence during carbenicillin treatment. Here we present a 3.7-Å resolution cryoelectron microscopy structure of LdcA. We introduce an original approach correlating phylogenetic signal with structural information and reveal possible recombination among LdcA and arginine decarboxylase subfamilies within structural domain boundaries. We show that LdcA is involved in full virulence in an insect pathogenesis model. Furthermore, unlike its enterobacterial counterparts, LdcA is regulated neither by the stringent response alarmone ppGpp nor by the AAA+ ATPase RavA. Instead, the P. aeruginosa ravA gene seems to play a defensive role. Altogether, our study identifies LdcA as an important player in P. aeruginosa physiology and virulence and as a potential drug target.

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