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Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features

Acinetobacter baumannii is an important causative agent of hospital acquired infections. In addition to acquired resistance to many currently-available antibiotics, it is intrinsically resistant to fosfomycin. It has previously been shown that AmpD and AnmK contribute to intrinsic fosfomycin resista...

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Autores principales: Tajuelo, Ana, Terrón, María C., López-Siles, Mireia, McConnell, Michael J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9880065/
https://www.ncbi.nlm.nih.gov/pubmed/36710969
http://dx.doi.org/10.3389/fcimb.2022.1064053
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author Tajuelo, Ana
Terrón, María C.
López-Siles, Mireia
McConnell, Michael J.
author_facet Tajuelo, Ana
Terrón, María C.
López-Siles, Mireia
McConnell, Michael J.
author_sort Tajuelo, Ana
collection PubMed
description Acinetobacter baumannii is an important causative agent of hospital acquired infections. In addition to acquired resistance to many currently-available antibiotics, it is intrinsically resistant to fosfomycin. It has previously been shown that AmpD and AnmK contribute to intrinsic fosfomycin resistance in A. baumannii due to their involvement in the peptidoglycan recycling pathway. However, the role that these two enzymes play in the fitness and virulence of A. baumannii has not been studied. The aim of this study was to characterize several virulence-related phenotypic traits in A. baumannii mutants lacking AmpD and AnmK. Specifically, cell morphology, peptidoglycan thickness, membrane permeability, growth under iron-limiting conditions, fitness, resistance to disinfectants and antimicrobial agents, twitching motility and biofilm formation of the mutant strains A. baumannii ATCC 17978 ΔampD::Kan and ΔanmK::Kan were compared to the wild type strain. Our results demonstrate that bacterial growth and fitness of both mutants were compromised, especially in the ΔampD::Kan mutant. In addition, biofilm formation was decreased by up to 69%, whereas twitching movement was reduced by about 80% in both mutants. These results demonstrate that, in addition to increased susceptibility to fosfomycin, alteration of the peptidoglycan recycling pathway affects multiple aspects related to virulence. Inhibition of these enzymes could be explored as a strategy to develop novel treatments for A. baumannii in the future. Furthermore, this study establishes a link between intrinsic fosfomycin resistance mechanisms and bacterial fitness and virulence traits.
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spelling pubmed-98800652023-01-28 Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features Tajuelo, Ana Terrón, María C. López-Siles, Mireia McConnell, Michael J. Front Cell Infect Microbiol Cellular and Infection Microbiology Acinetobacter baumannii is an important causative agent of hospital acquired infections. In addition to acquired resistance to many currently-available antibiotics, it is intrinsically resistant to fosfomycin. It has previously been shown that AmpD and AnmK contribute to intrinsic fosfomycin resistance in A. baumannii due to their involvement in the peptidoglycan recycling pathway. However, the role that these two enzymes play in the fitness and virulence of A. baumannii has not been studied. The aim of this study was to characterize several virulence-related phenotypic traits in A. baumannii mutants lacking AmpD and AnmK. Specifically, cell morphology, peptidoglycan thickness, membrane permeability, growth under iron-limiting conditions, fitness, resistance to disinfectants and antimicrobial agents, twitching motility and biofilm formation of the mutant strains A. baumannii ATCC 17978 ΔampD::Kan and ΔanmK::Kan were compared to the wild type strain. Our results demonstrate that bacterial growth and fitness of both mutants were compromised, especially in the ΔampD::Kan mutant. In addition, biofilm formation was decreased by up to 69%, whereas twitching movement was reduced by about 80% in both mutants. These results demonstrate that, in addition to increased susceptibility to fosfomycin, alteration of the peptidoglycan recycling pathway affects multiple aspects related to virulence. Inhibition of these enzymes could be explored as a strategy to develop novel treatments for A. baumannii in the future. Furthermore, this study establishes a link between intrinsic fosfomycin resistance mechanisms and bacterial fitness and virulence traits. Frontiers Media S.A. 2023-01-13 /pmc/articles/PMC9880065/ /pubmed/36710969 http://dx.doi.org/10.3389/fcimb.2022.1064053 Text en Copyright © 2023 Tajuelo, Terrón, López-Siles and McConnell https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cellular and Infection Microbiology
Tajuelo, Ana
Terrón, María C.
López-Siles, Mireia
McConnell, Michael J.
Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title_full Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title_fullStr Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title_full_unstemmed Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title_short Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features
title_sort role of peptidoglycan recycling enzymes ampd and anmk in acinetobacter baumannii virulence features
topic Cellular and Infection Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9880065/
https://www.ncbi.nlm.nih.gov/pubmed/36710969
http://dx.doi.org/10.3389/fcimb.2022.1064053
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