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dc.contributor.author | Tajuelo, Ana | |
dc.contributor.author | Terrón-Orellana, Maria Carmen | |
dc.contributor.author | Lopez-Siles, Mireia | |
dc.contributor.author | McConnell, Michael J | |
dc.date.accessioned | 2023-07-20T14:14:21Z | |
dc.date.available | 2023-07-20T14:14:21Z | |
dc.date.issued | 2023 | |
dc.identifier.citation | Front Cell Infect Microbiol. 2023 Jan 13;12:1064053. | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/16303 | |
dc.description.abstract | 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. | es_ES |
dc.description.sponsorship | ML-S was supported by the Sara Borrell Program of the Instituto de Salud Carlos III (CD17CIII/00017), and AT was supported by the Garantıa Juvenil Program of the Comunidad ́Autónoma de Madrid (PEJ2018-004820-A -MPY 387/19), is currently supported by a FPU grant (FPU20/03261) and PhD student in Biomedical Sciences and Public Health, Universidad Nacional de Educación a Distancia (UNED), Madrid, Spain (atajuelo11@alumno.uned.es). MM is supported by grants from the Instituto de Salud Carlos III (MP 516/19 and MPY 380/18). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Frontiers Media | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Acinetobacter baumannii | es_ES |
dc.subject | Peptidoglycan recycling | es_ES |
dc.subject | Biofilm formation | es_ES |
dc.subject | Twitching motility | es_ES |
dc.subject | Disinfectants | es_ES |
dc.subject | Fosfomycin resistance | es_ES |
dc.subject.mesh | Fosfomycin | es_ES |
dc.subject.mesh | Acinetobacter baumannii | es_ES |
dc.subject.mesh | Virulence | es_ES |
dc.subject.mesh | Peptidoglycan | es_ES |
dc.subject.mesh | Anti-Bacterial Agents | es_ES |
dc.subject.mesh | Biofilms | es_ES |
dc.subject.mesh | Drug Resistance, Multiple, Bacterial | es_ES |
dc.title | Role of peptidoglycan recycling enzymes AmpD and AnmK in Acinetobacter baumannii virulence features | es_ES |
dc.type | research article | es_ES |
dc.rights.license | Atribución 4.0 Internacional | * |
dc.identifier.pubmedID | 36710969 | es_ES |
dc.format.volume | 12 | es_ES |
dc.format.page | 1064053 | es_ES |
dc.identifier.doi | 10.3389/fcimb.2022.1064053 | es_ES |
dc.contributor.funder | Instituto de Salud Carlos III | es_ES |
dc.contributor.funder | Comunidad de Madrid (España) | es_ES |
dc.contributor.funder | National University of Distance Education (España) | es_ES |
dc.description.peerreviewed | Sí | es_ES |
dc.identifier.e-issn | 2235-2988 | es_ES |
dc.relation.publisherversion | https://doi.org/10.3389/fcimb.2022.1064053 | es_ES |
dc.identifier.journal | Frontiers in cellular and infection microbiology | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología::Unidades Comunes Científico-Técnicas (UCCT) | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.rights.accessRights | open access | es_ES |
dc.relation.projectFIS | info:eu-repo/grantAgreement/ES/CD17CIII/00017 | es_ES |
dc.relation.projectFIS | info:eu-repo/grantAgreement/ES/MP516/19 | es_ES |
dc.relation.projectFIS | info:eu-repo/grantAgreement/ES/MPY380/18 | es_ES |