Lipidated β-lactamases: from bench to bedside

Autores
Gonzalez, Lisandro Javier; Bahr, Guillermo; Vila, Alejandro Jose
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Carbapenemases represent one of the largest clinical threats to the action of carbapenems; the last resort drugs for the treatment of healthcare-associated infections caused by Gram-negative bacteria [1]. Metallo-β-lactamases (MBLs) are Zn(II)-dependent enzymes that constitute the largest family of carbapenemases of clinical impact. Among them, the New Delhi Metallo-β-lactamase (NDM-1) is a plasmid-encoded carbapenemase that has experienced the fastest and widest geographical spread, having been detected in more than 80 countries worldwide since its identification in 2008 [2]. Remarkably, the clinical success of this resistance determinant does not seem to be associated with the dissemination of a particular clone or genetic structure [3]. We have recently suggested that this particular success is due to the cellular localization of NDM-1: while all other known MBLs are soluble periplasmic proteins, NDM-1 is a lipoprotein anchored to the inner leaflet of the outer membrane in Gram-negative bacteria [4]. Despite NDM-1 being reported as a lipidated protein in 2011 [5], this fact was regarded as a biochemical curiosity and deserved little attention until recently when we reported that lipidation and membrane anchoring confer unique evolutionary advantages to NDM-1 [4].
Fil: Gonzalez, Lisandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Bahr, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
Antibiotic Resistance
Lipoproteins
Membrane-Anchoring
Ndm-1
Β-Lactamases
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/50584
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/50584
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Lipidated β-lactamases: from bench to bedsideGonzalez, Lisandro JavierBahr, GuillermoVila, Alejandro JoseAntibiotic ResistanceLipoproteinsMembrane-AnchoringNdm-1Β-Lactamaseshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Carbapenemases represent one of the largest clinical threats to the action of carbapenems; the last resort drugs for the treatment of healthcare-associated infections caused by Gram-negative bacteria [1]. Metallo-β-lactamases (MBLs) are Zn(II)-dependent enzymes that constitute the largest family of carbapenemases of clinical impact. Among them, the New Delhi Metallo-β-lactamase (NDM-1) is a plasmid-encoded carbapenemase that has experienced the fastest and widest geographical spread, having been detected in more than 80 countries worldwide since its identification in 2008 [2]. Remarkably, the clinical success of this resistance determinant does not seem to be associated with the dissemination of a particular clone or genetic structure [3]. We have recently suggested that this particular success is due to the cellular localization of NDM-1: while all other known MBLs are soluble periplasmic proteins, NDM-1 is a lipoprotein anchored to the inner leaflet of the outer membrane in Gram-negative bacteria [4]. Despite NDM-1 being reported as a lipidated protein in 2011 [5], this fact was regarded as a biochemical curiosity and deserved little attention until recently when we reported that lipidation and membrane anchoring confer unique evolutionary advantages to NDM-1 [4].Fil: Gonzalez, Lisandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Bahr, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFuture Medicine2016-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/50584Gonzalez, Lisandro Javier; Bahr, Guillermo; Vila, Alejandro Jose; Lipidated β-lactamases: from bench to bedside; Future Medicine; Future Microbiology; 11; 12; 12-2016; 1495-14981746-0913CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.2217/fmb-2016-0176info:eu-repo/semantics/altIdentifier/url/https://www.futuremedicine.com/doi/10.2217/fmb-2016-0176info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:47Zoai:ri.conicet.gov.ar:11336/50584instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:49:47.541CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Lipidated β-lactamases: from bench to bedside
title Lipidated β-lactamases: from bench to bedside
spellingShingle Lipidated β-lactamases: from bench to bedside
Gonzalez, Lisandro Javier
Antibiotic Resistance
Lipoproteins
Membrane-Anchoring
Ndm-1
Β-Lactamases
title_short Lipidated β-lactamases: from bench to bedside
title_full Lipidated β-lactamases: from bench to bedside
title_fullStr Lipidated β-lactamases: from bench to bedside
title_full_unstemmed Lipidated β-lactamases: from bench to bedside
title_sort Lipidated β-lactamases: from bench to bedside
dc.creator.none.fl_str_mv Gonzalez, Lisandro Javier
Bahr, Guillermo
Vila, Alejandro Jose
author Gonzalez, Lisandro Javier
author_facet Gonzalez, Lisandro Javier
Bahr, Guillermo
Vila, Alejandro Jose
author_role author
author2 Bahr, Guillermo
Vila, Alejandro Jose
author2_role author
author
dc.subject.none.fl_str_mv Antibiotic Resistance
Lipoproteins
Membrane-Anchoring
Ndm-1
Β-Lactamases
topic Antibiotic Resistance
Lipoproteins
Membrane-Anchoring
Ndm-1
Β-Lactamases
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Carbapenemases represent one of the largest clinical threats to the action of carbapenems; the last resort drugs for the treatment of healthcare-associated infections caused by Gram-negative bacteria [1]. Metallo-β-lactamases (MBLs) are Zn(II)-dependent enzymes that constitute the largest family of carbapenemases of clinical impact. Among them, the New Delhi Metallo-β-lactamase (NDM-1) is a plasmid-encoded carbapenemase that has experienced the fastest and widest geographical spread, having been detected in more than 80 countries worldwide since its identification in 2008 [2]. Remarkably, the clinical success of this resistance determinant does not seem to be associated with the dissemination of a particular clone or genetic structure [3]. We have recently suggested that this particular success is due to the cellular localization of NDM-1: while all other known MBLs are soluble periplasmic proteins, NDM-1 is a lipoprotein anchored to the inner leaflet of the outer membrane in Gram-negative bacteria [4]. Despite NDM-1 being reported as a lipidated protein in 2011 [5], this fact was regarded as a biochemical curiosity and deserved little attention until recently when we reported that lipidation and membrane anchoring confer unique evolutionary advantages to NDM-1 [4].
Fil: Gonzalez, Lisandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Bahr, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description Carbapenemases represent one of the largest clinical threats to the action of carbapenems; the last resort drugs for the treatment of healthcare-associated infections caused by Gram-negative bacteria [1]. Metallo-β-lactamases (MBLs) are Zn(II)-dependent enzymes that constitute the largest family of carbapenemases of clinical impact. Among them, the New Delhi Metallo-β-lactamase (NDM-1) is a plasmid-encoded carbapenemase that has experienced the fastest and widest geographical spread, having been detected in more than 80 countries worldwide since its identification in 2008 [2]. Remarkably, the clinical success of this resistance determinant does not seem to be associated with the dissemination of a particular clone or genetic structure [3]. We have recently suggested that this particular success is due to the cellular localization of NDM-1: while all other known MBLs are soluble periplasmic proteins, NDM-1 is a lipoprotein anchored to the inner leaflet of the outer membrane in Gram-negative bacteria [4]. Despite NDM-1 being reported as a lipidated protein in 2011 [5], this fact was regarded as a biochemical curiosity and deserved little attention until recently when we reported that lipidation and membrane anchoring confer unique evolutionary advantages to NDM-1 [4].
publishDate 2016
dc.date.none.fl_str_mv 2016-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/50584
Gonzalez, Lisandro Javier; Bahr, Guillermo; Vila, Alejandro Jose; Lipidated β-lactamases: from bench to bedside; Future Medicine; Future Microbiology; 11; 12; 12-2016; 1495-1498
1746-0913
CONICET Digital
CONICET
url http://hdl.handle.net/11336/50584
identifier_str_mv Gonzalez, Lisandro Javier; Bahr, Guillermo; Vila, Alejandro Jose; Lipidated β-lactamases: from bench to bedside; Future Medicine; Future Microbiology; 11; 12; 12-2016; 1495-1498
1746-0913
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2217/fmb-2016-0176
info:eu-repo/semantics/altIdentifier/url/https://www.futuremedicine.com/doi/10.2217/fmb-2016-0176
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Future Medicine
publisher.none.fl_str_mv Future Medicine
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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