Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae

Enterobacter cloacae starred different pioneer studies that enabled the development of a widely accepted model for the peptidoglycan metabolism-linked regulation of intrinsic class C cephalosporinases, highly conserved in different Gram-negatives. However, some mechanistic and fitness/virulence-rela...

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Autores: Barceló, Isabel María, Escobar-Salom, Maria, Jordana-Lluch, Elena, Torrens, Gabriel, Oliver, Antonio, Juan, Carlos
Tipo de documento: artigo
Data de publicação:2024
País:España
Recursos:Instituto de Salud Carlos III (ISCIII)
Repositório:Repisalud
Idioma:inglês
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/23830
Acesso em linha:https://hdl.handle.net/20.500.12105/23830
Access Level:Acceso aberto
Palavra-chave:Enterobacter cloacae
Pruebas de Sensibilidad Microbiana
Cefalosporinasa
Peptidoglicano
Proteínas Bacterianas
beta-Lactamasas
Resistencia betalactómica
Bacterial Proteins
beta-Lactam Resistance
Peptidoglycan
Microbial Sensitivity Tests
Cephalosporinase
beta-Lactamases
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spelling Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacaeBarceló, Isabel MaríaEscobar-Salom, MariaJordana-Lluch, ElenaTorrens, GabrielOliver, AntonioJuan, CarlosEnterobacter cloacaePruebas de Sensibilidad MicrobianaCefalosporinasaPeptidoglicanoProteínas Bacterianasbeta-LactamasasResistencia betalactómicaBacterial Proteinsbeta-Lactam ResistancePeptidoglycanMicrobial Sensitivity TestsCephalosporinasebeta-LactamasesEnterobacter cloacaeEnterobacter cloacae starred different pioneer studies that enabled the development of a widely accepted model for the peptidoglycan metabolism-linked regulation of intrinsic class C cephalosporinases, highly conserved in different Gram-negatives. However, some mechanistic and fitness/virulence-related aspects of E. cloacae choromosomal AmpC-dependent resistance are not completely understood. The present study including knockout mutants, β-lactamase cloning, gene expression analysis, characterization of resistance phenotypes, and the Galleria mellonella infection model fills these gaps demonstrating that: (i) AmpC enzyme does not show any collateral activity impacting fitness/virulence; (ii) AmpC hyperproduction mediated by ampD inactivation does not entail any biological cost; (iii) alteration of peptidoglycan recycling alone or combined with AmpC hyperproduction causes no attenuation of E. cloacae virulence in contrast to other species; (iv) derepression of E. cloacae AmpC does not follow a stepwise dynamics linked to the sequential inactivation of AmpD amidase homologues as happens in Pseudomonas aeruginosa; (v) the enigmatic additional putative AmpC-type β-lactamase generally present in E. cloacae does not contribute to the classical cephalosporinase hyperproduction-based resistance, having a negligible impact on phenotypes even when hyperproduced from multicopy vector. This study reveals interesting particularities in the chromosomal AmpC-related behavior of E. cloacae that complete the knowledge on this top resistance mechanism.Nature Publishing Group20242024-10-0920242024-01-0220242024-01-02research articlehttp://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articlehttps://hdl.handle.net/20.500.12105/23830reponame:Repisaludinstname:Instituto de Salud Carlos III (ISCIII)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repisalud.isciii.es:20.500.12105/238302026-06-12T12:43:37Z
dc.title.none.fl_str_mv Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
title Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
spellingShingle Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
Barceló, Isabel María
Enterobacter cloacae
Pruebas de Sensibilidad Microbiana
Cefalosporinasa
Peptidoglicano
Proteínas Bacterianas
beta-Lactamasas
Resistencia betalactómica
Bacterial Proteins
beta-Lactam Resistance
Peptidoglycan
Microbial Sensitivity Tests
Cephalosporinase
beta-Lactamases
Enterobacter cloacae
title_short Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
title_full Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
title_fullStr Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
title_full_unstemmed Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
title_sort Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae
dc.creator.none.fl_str_mv Barceló, Isabel María
Escobar-Salom, Maria
Jordana-Lluch, Elena
Torrens, Gabriel
Oliver, Antonio
Juan, Carlos
author Barceló, Isabel María
author_facet Barceló, Isabel María
Escobar-Salom, Maria
Jordana-Lluch, Elena
Torrens, Gabriel
Oliver, Antonio
Juan, Carlos
author_role author
author2 Escobar-Salom, Maria
Jordana-Lluch, Elena
Torrens, Gabriel
Oliver, Antonio
Juan, Carlos
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv Enterobacter cloacae
Pruebas de Sensibilidad Microbiana
Cefalosporinasa
Peptidoglicano
Proteínas Bacterianas
beta-Lactamasas
Resistencia betalactómica
Bacterial Proteins
beta-Lactam Resistance
Peptidoglycan
Microbial Sensitivity Tests
Cephalosporinase
beta-Lactamases
Enterobacter cloacae
topic Enterobacter cloacae
Pruebas de Sensibilidad Microbiana
Cefalosporinasa
Peptidoglicano
Proteínas Bacterianas
beta-Lactamasas
Resistencia betalactómica
Bacterial Proteins
beta-Lactam Resistance
Peptidoglycan
Microbial Sensitivity Tests
Cephalosporinase
beta-Lactamases
Enterobacter cloacae
description Enterobacter cloacae starred different pioneer studies that enabled the development of a widely accepted model for the peptidoglycan metabolism-linked regulation of intrinsic class C cephalosporinases, highly conserved in different Gram-negatives. However, some mechanistic and fitness/virulence-related aspects of E. cloacae choromosomal AmpC-dependent resistance are not completely understood. The present study including knockout mutants, β-lactamase cloning, gene expression analysis, characterization of resistance phenotypes, and the Galleria mellonella infection model fills these gaps demonstrating that: (i) AmpC enzyme does not show any collateral activity impacting fitness/virulence; (ii) AmpC hyperproduction mediated by ampD inactivation does not entail any biological cost; (iii) alteration of peptidoglycan recycling alone or combined with AmpC hyperproduction causes no attenuation of E. cloacae virulence in contrast to other species; (iv) derepression of E. cloacae AmpC does not follow a stepwise dynamics linked to the sequential inactivation of AmpD amidase homologues as happens in Pseudomonas aeruginosa; (v) the enigmatic additional putative AmpC-type β-lactamase generally present in E. cloacae does not contribute to the classical cephalosporinase hyperproduction-based resistance, having a negligible impact on phenotypes even when hyperproduced from multicopy vector. This study reveals interesting particularities in the chromosomal AmpC-related behavior of E. cloacae that complete the knowledge on this top resistance mechanism.
publishDate 2024
dc.date.none.fl_str_mv 2024
2024-10-09
2024
2024-01-02
2024
2024-01-02
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.12105/23830
url https://hdl.handle.net/20.500.12105/23830
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:Repisalud
instname:Instituto de Salud Carlos III (ISCIII)
instname_str Instituto de Salud Carlos III (ISCIII)
reponame_str Repisalud
collection Repisalud
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869405495288135680
score 15,81155

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