In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase

Autores
Moran Barrio, Jorgelina; Lisa, María Natalia; Vila, Alejandro Jose
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Metallo- -lactamases (M Ls) represent one of the main mechanisms of bacterial resistance against -lactam antibiotics. The elucidation of their mechanism has been limited mostly by the structural diversity among their active sites. All M Ls structurally characterized so far present a Cys or a Ser residue at position 221, which is critical for catalysis. GOB lactamases stand as an exception within this picture, possessing a Met residue in this location. We studied different mutants in this position, and we show that Met221 is essential for protein stability, most likely due to its involvement in a hydrophobic core. In contrast to other known M Ls, residue 221 is not involved in metal binding or in catalysis in GOB enzymes, further highlighting the structural diversity of M Ls. We also demonstrate the usefulness of protein periplasmic profiles to assess the contribution of protein stability to antibiotic resistance.
Fil: Moran Barrio, Jorgelina. 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: Lisa, María Natalia. 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
Metallo-beta-lactamases
Bacterial resistance
GOB enzymes
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:11336/269358
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling In Vivo Impact of Met221 Substitution in GOB Metallo-β-LactamaseMoran Barrio, JorgelinaLisa, María NataliaVila, Alejandro JoseMetallo-beta-lactamasesBacterial resistanceGOB enzymeshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Metallo- -lactamases (M Ls) represent one of the main mechanisms of bacterial resistance against -lactam antibiotics. The elucidation of their mechanism has been limited mostly by the structural diversity among their active sites. All M Ls structurally characterized so far present a Cys or a Ser residue at position 221, which is critical for catalysis. GOB lactamases stand as an exception within this picture, possessing a Met residue in this location. We studied different mutants in this position, and we show that Met221 is essential for protein stability, most likely due to its involvement in a hydrophobic core. In contrast to other known M Ls, residue 221 is not involved in metal binding or in catalysis in GOB enzymes, further highlighting the structural diversity of M Ls. We also demonstrate the usefulness of protein periplasmic profiles to assess the contribution of protein stability to antibiotic resistance.Fil: Moran Barrio, Jorgelina. 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: Lisa, María Natalia. 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; ArgentinaAmerican Society for Microbiology2012-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/269358Moran Barrio, Jorgelina; Lisa, María Natalia; Vila, Alejandro Jose; In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 56; 4; 1-2012; 1769-17730066-4804CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.asm.org/doi/10.1128/aac.05418-11info:eu-repo/semantics/altIdentifier/doi/10.1128/AAC.05418-11info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:29:48Zoai:ri.conicet.gov.ar:11336/269358instacron: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 10:29:48.814CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
title In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
spellingShingle In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
Moran Barrio, Jorgelina
Metallo-beta-lactamases
Bacterial resistance
GOB enzymes
title_short In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
title_full In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
title_fullStr In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
title_full_unstemmed In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
title_sort In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase
dc.creator.none.fl_str_mv Moran Barrio, Jorgelina
Lisa, María Natalia
Vila, Alejandro Jose
author Moran Barrio, Jorgelina
author_facet Moran Barrio, Jorgelina
Lisa, María Natalia
Vila, Alejandro Jose
author_role author
author2 Lisa, María Natalia
Vila, Alejandro Jose
author2_role author
author
dc.subject.none.fl_str_mv Metallo-beta-lactamases
Bacterial resistance
GOB enzymes
topic Metallo-beta-lactamases
Bacterial resistance
GOB enzymes
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Metallo- -lactamases (M Ls) represent one of the main mechanisms of bacterial resistance against -lactam antibiotics. The elucidation of their mechanism has been limited mostly by the structural diversity among their active sites. All M Ls structurally characterized so far present a Cys or a Ser residue at position 221, which is critical for catalysis. GOB lactamases stand as an exception within this picture, possessing a Met residue in this location. We studied different mutants in this position, and we show that Met221 is essential for protein stability, most likely due to its involvement in a hydrophobic core. In contrast to other known M Ls, residue 221 is not involved in metal binding or in catalysis in GOB enzymes, further highlighting the structural diversity of M Ls. We also demonstrate the usefulness of protein periplasmic profiles to assess the contribution of protein stability to antibiotic resistance.
Fil: Moran Barrio, Jorgelina. 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: Lisa, María Natalia. 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 Metallo- -lactamases (M Ls) represent one of the main mechanisms of bacterial resistance against -lactam antibiotics. The elucidation of their mechanism has been limited mostly by the structural diversity among their active sites. All M Ls structurally characterized so far present a Cys or a Ser residue at position 221, which is critical for catalysis. GOB lactamases stand as an exception within this picture, possessing a Met residue in this location. We studied different mutants in this position, and we show that Met221 is essential for protein stability, most likely due to its involvement in a hydrophobic core. In contrast to other known M Ls, residue 221 is not involved in metal binding or in catalysis in GOB enzymes, further highlighting the structural diversity of M Ls. We also demonstrate the usefulness of protein periplasmic profiles to assess the contribution of protein stability to antibiotic resistance.
publishDate 2012
dc.date.none.fl_str_mv 2012-01
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/11336/269358
Moran Barrio, Jorgelina; Lisa, María Natalia; Vila, Alejandro Jose; In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 56; 4; 1-2012; 1769-1773
0066-4804
CONICET Digital
CONICET
url http://hdl.handle.net/11336/269358
identifier_str_mv Moran Barrio, Jorgelina; Lisa, María Natalia; Vila, Alejandro Jose; In Vivo Impact of Met221 Substitution in GOB Metallo-β-Lactamase; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 56; 4; 1-2012; 1769-1773
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.05418-11
info:eu-repo/semantics/altIdentifier/doi/10.1128/AAC.05418-11
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
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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