Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity

Autores
Salvucci, Emiliano Jesus; Saavedra, Maria Lucila; Sesma, Fernando Juan Manuel
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Objectives: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43- amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties. Methods: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to evaluate the dissipation of membrane potentials in intact cells were carried out. Time-kill kinetics of Listeria innocua cells with the active peptide were performed. Results and conclusions: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial activities.
Fil: Salvucci, Emiliano Jesus. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Materia
Enterococci
Liposomes
Pediocin
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:11336/56486
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/56486
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activitySalvucci, Emiliano JesusSaavedra, Maria LucilaSesma, Fernando Juan ManuelEnterococciLiposomesPediocinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Objectives: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43- amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties. Methods: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to evaluate the dissipation of membrane potentials in intact cells were carried out. Time-kill kinetics of Listeria innocua cells with the active peptide were performed. Results and conclusions: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial activities.Fil: Salvucci, Emiliano Jesus. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaOxford University Press2007-06-21info: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/11336/56486Salvucci, Emiliano Jesus; Saavedra, Maria Lucila; Sesma, Fernando Juan Manuel; Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity; Oxford University Press; Journal of Antimicrobial Chemotherapy; 59; 6; 21-6-2007; 1102-11080305-74531460-2091CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/jac/dkm096info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jac/article/59/6/1102/713969info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:42:55Zoai:ri.conicet.gov.ar:11336/56486instacron: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:34982025-10-22 11:42:55.505CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
title Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
spellingShingle Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
Salvucci, Emiliano Jesus
Enterococci
Liposomes
Pediocin
title_short Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
title_full Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
title_fullStr Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
title_full_unstemmed Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
title_sort Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
dc.creator.none.fl_str_mv Salvucci, Emiliano Jesus
Saavedra, Maria Lucila
Sesma, Fernando Juan Manuel
author Salvucci, Emiliano Jesus
author_facet Salvucci, Emiliano Jesus
Saavedra, Maria Lucila
Sesma, Fernando Juan Manuel
author_role author
author2 Saavedra, Maria Lucila
Sesma, Fernando Juan Manuel
author2_role author
author
dc.subject.none.fl_str_mv Enterococci
Liposomes
Pediocin
topic Enterococci
Liposomes
Pediocin
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Objectives: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43- amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties. Methods: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to evaluate the dissipation of membrane potentials in intact cells were carried out. Time-kill kinetics of Listeria innocua cells with the active peptide were performed. Results and conclusions: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial activities.
Fil: Salvucci, Emiliano Jesus. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
description Objectives: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43- amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties. Methods: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to evaluate the dissipation of membrane potentials in intact cells were carried out. Time-kill kinetics of Listeria innocua cells with the active peptide were performed. Results and conclusions: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial activities.
publishDate 2007
dc.date.none.fl_str_mv 2007-06-21
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/11336/56486
Salvucci, Emiliano Jesus; Saavedra, Maria Lucila; Sesma, Fernando Juan Manuel; Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity; Oxford University Press; Journal of Antimicrobial Chemotherapy; 59; 6; 21-6-2007; 1102-1108
0305-7453
1460-2091
CONICET Digital
CONICET
url http://hdl.handle.net/11336/56486
identifier_str_mv Salvucci, Emiliano Jesus; Saavedra, Maria Lucila; Sesma, Fernando Juan Manuel; Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity; Oxford University Press; Journal of Antimicrobial Chemotherapy; 59; 6; 21-6-2007; 1102-1108
0305-7453
1460-2091
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/jac/dkm096
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jac/article/59/6/1102/713969
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
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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_ 1846782118532743168
score 12.982451

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