Structure, function, and evolution of the pseudomonas aeruginosa lysine decarboxylase LdcA

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

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1842-1854.e4
Issue number12
Early online date22 Oct 2019
Publication statusPublished - 3 Dec 2019

Bibliographical note

Copyright © 2019 Elsevier Ltd. All rights reserved.


  • LdcA
  • Pseudomonas aeruginosa
  • amino acid decarboxylases
  • bacteria
  • cryo-EM structure
  • defense island
  • evolution
  • phylogenetic analysis
  • ppGpp
  • virulence

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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