Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum

Enterocin C (EntC), a class IIb bacteriocin was purified from culture supernatants of Enterococcus faecalis C901, a strain isolated from human colostrum. Enterocin C consists of two distinct peptides, named EntC1 and EntC2, whose complementary action is required for full antimicrobial activity. The...

ver descrição completa

Detalhes bibliográficos
Autores: Maldonado-Barragán, Antonio, Caballero-Guerrero, Belén, Jiménez, Esther, Jiménez Díaz, Rufino, Ruiz-Barba, José Luis, Rodríguez, Juan M.
Formato: artículo
Fecha de publicación:2009
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/23842
Acesso em linha:http://hdl.handle.net/10261/23842
Access Level:acceso abierto
Palavra-chave:Enterocin
Two-peptide bacteriocin
Breast milk
Colostrum
id ES_9be71a319d7247f40d9333da3dfd360d
oai_identifier_str oai:digital.csic.es:10261/23842
network_acronym_str ES
network_name_str España
repository_id_str
spelling Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human ColostrumMaldonado-Barragán, AntonioCaballero-Guerrero, BelénJiménez, EstherJiménez Díaz, RufinoRuiz-Barba, José LuisRodríguez, Juan M.EnterocinTwo-peptide bacteriocinBreast milkColostrumEnterocin C (EntC), a class IIb bacteriocin was purified from culture supernatants of Enterococcus faecalis C901, a strain isolated from human colostrum. Enterocin C consists of two distinct peptides, named EntC1 and EntC2, whose complementary action is required for full antimicrobial activity. The structural genes entC1 and entC2 encoding enterocins EntC1 and EntC2, respectively, and that encoding the putative immunity protein (EntCI) are located in the 9-kb plasmid pEntC, harboured by E. faecalis C901. The N-terminal sequence of both antimicrobial peptides revealed that EntC1 (4284 Da) is identical to Ent1071A, one of the two peptides that form enterocin 1071 (Ent1071), a bacteriocin produced by E. faecalis BFE 1071. In contrast, EntC2 (3867 Da) presents the non-polar alanine residue at position 17 (Ala17) instead of the polar threonine residue (Thr17) in Ent1071B, the second peptide constituting Ent1071. In spite of peptide similarities, EntC differs from Ent1071 in major aspects, including the complementary activity among its constitutive peptides and its wider inhibitory spectrum of activity. Different amphiphilic α-helical conformations between EntC2 and Ent1071B could explain both, acquired complementary activity and increased antimicrobial spectrum.This work was supported by the FUN-C-FOOD (Consolider-Ingenio 2010), AGL2006-00763 and AGL2007-62042 projects from the Ministerio de Educación y Ciencia (Spain). A. M. was the recipient of a post-doctoral grant (MEC-Fulbright program) from the Ministerio de Educación y Ciencia (MEC).Peer reviewed201020102009info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501691210 bytesapplication/pdfhttp://hdl.handle.net/10261/23842reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.ijfoodmicro.2009.05.008info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/238422026-05-22T06:33:51Z
dc.title.none.fl_str_mv Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
title Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
spellingShingle Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
Maldonado-Barragán, Antonio
Enterocin
Two-peptide bacteriocin
Breast milk
Colostrum
title_short Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
title_full Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
title_fullStr Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
title_full_unstemmed Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
title_sort Enterocin C, a Class IIb Bacteriocin Produced by E. faecalis C901, a Strain Isolated from Human Colostrum
dc.creator.none.fl_str_mv Maldonado-Barragán, Antonio
Caballero-Guerrero, Belén
Jiménez, Esther
Jiménez Díaz, Rufino
Ruiz-Barba, José Luis
Rodríguez, Juan M.
author Maldonado-Barragán, Antonio
author_facet Maldonado-Barragán, Antonio
Caballero-Guerrero, Belén
Jiménez, Esther
Jiménez Díaz, Rufino
Ruiz-Barba, José Luis
Rodríguez, Juan M.
author_role author
author2 Caballero-Guerrero, Belén
Jiménez, Esther
Jiménez Díaz, Rufino
Ruiz-Barba, José Luis
Rodríguez, Juan M.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Enterocin
Two-peptide bacteriocin
Breast milk
Colostrum
topic Enterocin
Two-peptide bacteriocin
Breast milk
Colostrum
description Enterocin C (EntC), a class IIb bacteriocin was purified from culture supernatants of Enterococcus faecalis C901, a strain isolated from human colostrum. Enterocin C consists of two distinct peptides, named EntC1 and EntC2, whose complementary action is required for full antimicrobial activity. The structural genes entC1 and entC2 encoding enterocins EntC1 and EntC2, respectively, and that encoding the putative immunity protein (EntCI) are located in the 9-kb plasmid pEntC, harboured by E. faecalis C901. The N-terminal sequence of both antimicrobial peptides revealed that EntC1 (4284 Da) is identical to Ent1071A, one of the two peptides that form enterocin 1071 (Ent1071), a bacteriocin produced by E. faecalis BFE 1071. In contrast, EntC2 (3867 Da) presents the non-polar alanine residue at position 17 (Ala17) instead of the polar threonine residue (Thr17) in Ent1071B, the second peptide constituting Ent1071. In spite of peptide similarities, EntC differs from Ent1071 in major aspects, including the complementary activity among its constitutive peptides and its wider inhibitory spectrum of activity. Different amphiphilic α-helical conformations between EntC2 and Ent1071B could explain both, acquired complementary activity and increased antimicrobial spectrum.
publishDate 2009
dc.date.none.fl_str_mv 2009
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/23842
url http://hdl.handle.net/10261/23842
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.ijfoodmicro.2009.05.008
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 691210 bytes
application/pdf
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869414611118194688
score 15,81155

Registos relacionados