Aminoglycoside modifying enzymes

Autores
Ramirez, Maria Soledad; Tolmasky, Marcelo E.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aminoglycosides have been an essential component of the armamentarium in the treatment of life-threatening infections. Unfortunately, their efficacy has been reduced by the surge and dissemination of resistance. In some cases the levels of resistance reached the point that rendered them virtually useless. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevalent in the clinical setting. Aminoglycoside modifying enzymes catalyze the modification at different -OH or -NH2 groups of the 2-deoxystreptamine nucleus or the sugar moieties and can be nucleotidyltranferases, phosphotransferases, or acetyltransferases. The number of aminoglycoside modifying enzymes identified to date as well as the genetic environments where the coding genes are located is impressive and there is virtually no bacteria that is unable to support enzymatic resistance to aminoglycosides. Aside from the development of new aminoglycosides refractory to as many as possible modifying enzymes there are currently two main strategies being pursued to overcome the action of aminoglycoside modifying enzymes. Their successful development would extend the useful life of existing antibiotics that have proven effective in the treatment of infections. These strategies consist of the development of inhibitors of the enzymatic action or of the expression of the modifying enzymes.
Fil: Ramirez, Maria Soledad. California State University Fullerton; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; Argentina
Fil: Tolmasky, Marcelo E.. California State University Fullerton; Estados Unidos
Materia
ACETYLTRANSFERASE
AMINOGLYCOSIDE
AMINOGLYCOSIDE MODIFYING ENZYME
ANTIBIOTIC RESISTANCE
ANTISENSE
BACTERIAL INFECTION
KINASE
NUCLEOTIDYLTRANSFERASE
PHOSPHOTRANSFERASE
RNASE H
RNASE P
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/67587
Acceder
id CONICETDig_bd9f25c25695d3ff9f6ea1cb6d67c1d5
oai_identifier_str oai:ri.conicet.gov.ar:11336/67587
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aminoglycoside modifying enzymesRamirez, Maria SoledadTolmasky, Marcelo E.ACETYLTRANSFERASEAMINOGLYCOSIDEAMINOGLYCOSIDE MODIFYING ENZYMEANTIBIOTIC RESISTANCEANTISENSEBACTERIAL INFECTIONKINASENUCLEOTIDYLTRANSFERASEPHOSPHOTRANSFERASERNASE HRNASE Phttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Aminoglycosides have been an essential component of the armamentarium in the treatment of life-threatening infections. Unfortunately, their efficacy has been reduced by the surge and dissemination of resistance. In some cases the levels of resistance reached the point that rendered them virtually useless. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevalent in the clinical setting. Aminoglycoside modifying enzymes catalyze the modification at different -OH or -NH2 groups of the 2-deoxystreptamine nucleus or the sugar moieties and can be nucleotidyltranferases, phosphotransferases, or acetyltransferases. The number of aminoglycoside modifying enzymes identified to date as well as the genetic environments where the coding genes are located is impressive and there is virtually no bacteria that is unable to support enzymatic resistance to aminoglycosides. Aside from the development of new aminoglycosides refractory to as many as possible modifying enzymes there are currently two main strategies being pursued to overcome the action of aminoglycoside modifying enzymes. Their successful development would extend the useful life of existing antibiotics that have proven effective in the treatment of infections. These strategies consist of the development of inhibitors of the enzymatic action or of the expression of the modifying enzymes.Fil: Ramirez, Maria Soledad. California State University Fullerton; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Tolmasky, Marcelo E.. California State University Fullerton; Estados UnidosChurchill Livingstone2010-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/67587Ramirez, Maria Soledad; Tolmasky, Marcelo E.; Aminoglycoside modifying enzymes; Churchill Livingstone; Drug Resistance Updates; 13; 6; 9-2010; 151-1711368-7646CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.drup.2010.08.003info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1368764610000385info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2992599/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:50:31Zoai:ri.conicet.gov.ar:11336/67587instacron: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 09:50:32.008CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aminoglycoside modifying enzymes
title Aminoglycoside modifying enzymes
spellingShingle Aminoglycoside modifying enzymes
Ramirez, Maria Soledad
ACETYLTRANSFERASE
AMINOGLYCOSIDE
AMINOGLYCOSIDE MODIFYING ENZYME
ANTIBIOTIC RESISTANCE
ANTISENSE
BACTERIAL INFECTION
KINASE
NUCLEOTIDYLTRANSFERASE
PHOSPHOTRANSFERASE
RNASE H
RNASE P
title_short Aminoglycoside modifying enzymes
title_full Aminoglycoside modifying enzymes
title_fullStr Aminoglycoside modifying enzymes
title_full_unstemmed Aminoglycoside modifying enzymes
title_sort Aminoglycoside modifying enzymes
dc.creator.none.fl_str_mv Ramirez, Maria Soledad
Tolmasky, Marcelo E.
author Ramirez, Maria Soledad
author_facet Ramirez, Maria Soledad
Tolmasky, Marcelo E.
author_role author
author2 Tolmasky, Marcelo E.
author2_role author
dc.subject.none.fl_str_mv ACETYLTRANSFERASE
AMINOGLYCOSIDE
AMINOGLYCOSIDE MODIFYING ENZYME
ANTIBIOTIC RESISTANCE
ANTISENSE
BACTERIAL INFECTION
KINASE
NUCLEOTIDYLTRANSFERASE
PHOSPHOTRANSFERASE
RNASE H
RNASE P
topic ACETYLTRANSFERASE
AMINOGLYCOSIDE
AMINOGLYCOSIDE MODIFYING ENZYME
ANTIBIOTIC RESISTANCE
ANTISENSE
BACTERIAL INFECTION
KINASE
NUCLEOTIDYLTRANSFERASE
PHOSPHOTRANSFERASE
RNASE H
RNASE P
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Aminoglycosides have been an essential component of the armamentarium in the treatment of life-threatening infections. Unfortunately, their efficacy has been reduced by the surge and dissemination of resistance. In some cases the levels of resistance reached the point that rendered them virtually useless. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevalent in the clinical setting. Aminoglycoside modifying enzymes catalyze the modification at different -OH or -NH2 groups of the 2-deoxystreptamine nucleus or the sugar moieties and can be nucleotidyltranferases, phosphotransferases, or acetyltransferases. The number of aminoglycoside modifying enzymes identified to date as well as the genetic environments where the coding genes are located is impressive and there is virtually no bacteria that is unable to support enzymatic resistance to aminoglycosides. Aside from the development of new aminoglycosides refractory to as many as possible modifying enzymes there are currently two main strategies being pursued to overcome the action of aminoglycoside modifying enzymes. Their successful development would extend the useful life of existing antibiotics that have proven effective in the treatment of infections. These strategies consist of the development of inhibitors of the enzymatic action or of the expression of the modifying enzymes.
Fil: Ramirez, Maria Soledad. California State University Fullerton; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; Argentina
Fil: Tolmasky, Marcelo E.. California State University Fullerton; Estados Unidos
description Aminoglycosides have been an essential component of the armamentarium in the treatment of life-threatening infections. Unfortunately, their efficacy has been reduced by the surge and dissemination of resistance. In some cases the levels of resistance reached the point that rendered them virtually useless. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevalent in the clinical setting. Aminoglycoside modifying enzymes catalyze the modification at different -OH or -NH2 groups of the 2-deoxystreptamine nucleus or the sugar moieties and can be nucleotidyltranferases, phosphotransferases, or acetyltransferases. The number of aminoglycoside modifying enzymes identified to date as well as the genetic environments where the coding genes are located is impressive and there is virtually no bacteria that is unable to support enzymatic resistance to aminoglycosides. Aside from the development of new aminoglycosides refractory to as many as possible modifying enzymes there are currently two main strategies being pursued to overcome the action of aminoglycoside modifying enzymes. Their successful development would extend the useful life of existing antibiotics that have proven effective in the treatment of infections. These strategies consist of the development of inhibitors of the enzymatic action or of the expression of the modifying enzymes.
publishDate 2010
dc.date.none.fl_str_mv 2010-09
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/11336/67587
Ramirez, Maria Soledad; Tolmasky, Marcelo E.; Aminoglycoside modifying enzymes; Churchill Livingstone; Drug Resistance Updates; 13; 6; 9-2010; 151-171
1368-7646
CONICET Digital
CONICET
url http://hdl.handle.net/11336/67587
identifier_str_mv Ramirez, Maria Soledad; Tolmasky, Marcelo E.; Aminoglycoside modifying enzymes; Churchill Livingstone; Drug Resistance Updates; 13; 6; 9-2010; 151-171
1368-7646
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.drup.2010.08.003
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1368764610000385
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2992599/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Churchill Livingstone
publisher.none.fl_str_mv Churchill Livingstone
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
_version_ 1842269036009750528
score 13.13397

Publicaciones similares