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

Lookup NU author(s): Manuel Banzhaf

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Abstract

© 2019 Elsevier LtdKandiah et al. solve the structure of the lysine decarboxylase LdcA from a human pathogen Pseudomonas aeruginosa by cryo-EM. They use evolutionary information to analyze the system, demonstrate involvement of LdcA in full virulence of the pathogen in vivo, and propose to target this protein for therapeutic interventions.© 2019 Elsevier LtdThe 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.

Publication metadata

Author(s): Kandiah E, Carriel D, Garcia PS, Felix J, Banzhaf M, Kritikos G, Bacia-Verloop M, Brochier-Armanet C, Elsen S, Gutsche I

Publication type: Article

Publication status: Published

Journal: Structure

Year: 2019

Volume: 27

Issue: 12

Pages: 1842-1854.e4

Print publication date: 03/12/2019

Online publication date: 22/10/2019

Acceptance date: 01/10/2019

ISSN (print): 0969-2126

ISSN (electronic): 1878-4186

Publisher: Cell Press

URL: https://doi.org/10.1016/j.str.2019.10.003

DOI: 10.1016/j.str.2019.10.003

PubMed id: 31653338

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