All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis

Autores
Amoroso, Ana Maria; Demares, Diego; Mollerach, Marta Eugenia; Gutkind, Gabriel Osvaldo; Coyette, Jacques
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the b-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 mg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.
Fil: Amoroso, Ana Maria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Demares, Diego. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Mollerach, Marta Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Coyette, Jacques. Université de Liège; Bélgica
Materia
Streptococcus
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:11336/154016
Acceder
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network_name_str CONICET Digital (CONICET)
spelling All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitisAmoroso, Ana MariaDemares, DiegoMollerach, Marta EugeniaGutkind, Gabriel OsvaldoCoyette, JacquesStreptococcushttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the b-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 mg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.Fil: Amoroso, Ana Maria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Demares, Diego. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Mollerach, Marta Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Coyette, Jacques. Université de Liège; BélgicaAmerican Society for Microbiology2001-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/154016Amoroso, Ana Maria; Demares, Diego; Mollerach, Marta Eugenia; Gutkind, Gabriel Osvaldo; Coyette, Jacques; All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 45; 7; 7-2001; 2075-20810066-4804CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.asm.org/doi/10.1128/AAC.45.7.2075-2081.2001info:eu-repo/semantics/altIdentifier/doi/10.1128/AAC.45.7.2075-2081.2001info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:20Zoai:ri.conicet.gov.ar:11336/154016instacron: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:34982025-09-29 09:37:20.231CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
title All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
spellingShingle All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
Amoroso, Ana Maria
Streptococcus
title_short All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
title_full All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
title_fullStr All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
title_full_unstemmed All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
title_sort All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis
dc.creator.none.fl_str_mv Amoroso, Ana Maria
Demares, Diego
Mollerach, Marta Eugenia
Gutkind, Gabriel Osvaldo
Coyette, Jacques
author Amoroso, Ana Maria
author_facet Amoroso, Ana Maria
Demares, Diego
Mollerach, Marta Eugenia
Gutkind, Gabriel Osvaldo
Coyette, Jacques
author_role author
author2 Demares, Diego
Mollerach, Marta Eugenia
Gutkind, Gabriel Osvaldo
Coyette, Jacques
author2_role author
author
author
author
dc.subject.none.fl_str_mv Streptococcus
topic Streptococcus
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the b-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 mg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.
Fil: Amoroso, Ana Maria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Demares, Diego. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Mollerach, Marta Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Coyette, Jacques. Université de Liège; Bélgica
description All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the b-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 mg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.
publishDate 2001
dc.date.none.fl_str_mv 2001-07
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/11336/154016
Amoroso, Ana Maria; Demares, Diego; Mollerach, Marta Eugenia; Gutkind, Gabriel Osvaldo; Coyette, Jacques; All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 45; 7; 7-2001; 2075-2081
0066-4804
CONICET Digital
CONICET
url http://hdl.handle.net/11336/154016
identifier_str_mv Amoroso, Ana Maria; Demares, Diego; Mollerach, Marta Eugenia; Gutkind, Gabriel Osvaldo; Coyette, Jacques; All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 45; 7; 7-2001; 2075-2081
0066-4804
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://journals.asm.org/doi/10.1128/AAC.45.7.2075-2081.2001
info:eu-repo/semantics/altIdentifier/doi/10.1128/AAC.45.7.2075-2081.2001
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
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
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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score 13.070432

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