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
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/56486
Ver los metadatos del registro completo
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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 |
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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 |
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eng |
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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 |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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openAccess |
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https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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application/pdf application/pdf application/pdf |
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Oxford University Press |
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Oxford University Press |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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