The ability to produce a metallophore that can extract the metal from zinc-binding proteins contributes to the remarkable ability of Pseudomona aeruginosa to proliferate in zinc-poor environments.Pseudomonas aeruginosa is known to exhibit considerable resistance to the antimicrobial activity of the metal-sequestering protein calprotectin (CP). In this study, we demonstrate that although CP induces zinc deficiency in P. aeruginosa, a strain unable to import zinc through the two most important metal acquisition systems, namely ZnuABC and ZrmABCD, maintains significant growth capacity in the presence of high concentrations of CP. Furthermore, we have shown that nicotianamine, a molecule structurally similar to the metallophore pseudopaline, can favor the acquisition of the metal even in the presence of CP. To gain insights into the mechanisms through which metallophores can promote zinc acquisition, we analyzed the effect of nicotianamine on the activity of the metallo-beta-lactamase VIM-1. Our data suggest that metallophores released by bacteria in response to zinc deficiency can extract the protein-bound metal. The ability to interfere with the binding of metals to proteins, as well as favoring the acquisition of zinc, may contribute to increasing the resistance of P. aeruginosa to the antimicrobial action of CP.

Ammendola, S., Secli, V., Pacello, F., Mastropasqua, M.c., Romão, M.a., Gomes, C.m., et al. (2022). Zinc-binding metallophores protect Pseudomonas aeruginosa from calprotectin-mediated metal starvation. FEMS MICROBIOLOGY LETTERS, 369(1) [10.1093/femsle/fnac071].

Zinc-binding metallophores protect Pseudomonas aeruginosa from calprotectin-mediated metal starvation

Ammendola, Serena;Pacello, Francesca;Mastropasqua, Maria Chiara;Battistoni, Andrea
2022-08-16

Abstract

The ability to produce a metallophore that can extract the metal from zinc-binding proteins contributes to the remarkable ability of Pseudomona aeruginosa to proliferate in zinc-poor environments.Pseudomonas aeruginosa is known to exhibit considerable resistance to the antimicrobial activity of the metal-sequestering protein calprotectin (CP). In this study, we demonstrate that although CP induces zinc deficiency in P. aeruginosa, a strain unable to import zinc through the two most important metal acquisition systems, namely ZnuABC and ZrmABCD, maintains significant growth capacity in the presence of high concentrations of CP. Furthermore, we have shown that nicotianamine, a molecule structurally similar to the metallophore pseudopaline, can favor the acquisition of the metal even in the presence of CP. To gain insights into the mechanisms through which metallophores can promote zinc acquisition, we analyzed the effect of nicotianamine on the activity of the metallo-beta-lactamase VIM-1. Our data suggest that metallophores released by bacteria in response to zinc deficiency can extract the protein-bound metal. The ability to interfere with the binding of metals to proteins, as well as favoring the acquisition of zinc, may contribute to increasing the resistance of P. aeruginosa to the antimicrobial action of CP.
16-ago-2022
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10 - BIOCHIMICA
Settore BIO/19 - MICROBIOLOGIA GENERALE
English
Pseudomonas aeruginosa
calprotectin
metallo-β-lactamase inhibition
metallophores
pseudopaline
zinc import
Ammendola, S., Secli, V., Pacello, F., Mastropasqua, M.c., Romão, M.a., Gomes, C.m., et al. (2022). Zinc-binding metallophores protect Pseudomonas aeruginosa from calprotectin-mediated metal starvation. FEMS MICROBIOLOGY LETTERS, 369(1) [10.1093/femsle/fnac071].
Ammendola, S; Secli, V; Pacello, F; Mastropasqua, Mc; Romão, Ma; Gomes, Cm; Battistoni, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/310776
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