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Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1

A bacteriocin-producing bacterium was isolated from boza and identified as Leuconostoc pseudomesenteroides KM432Bz. The antimicrobial peptide was purified and shown to be identical to other class IIa bacteriocins: leucocin A from Leuconostoc gelidum UAL-187 and Leuconostoc pseudomesenteroides QU15 a...

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Autores principales: Makhloufi, Kahina Maya, Carré-Mlouka, Alyssa, Peduzzi, Jean, Lombard, Carine, van Reenen, Carol Ann, Dicks, Leon Milner Theodore, Rebuffat, Sylvie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3731274/
https://www.ncbi.nlm.nih.gov/pubmed/23936441
http://dx.doi.org/10.1371/journal.pone.0070484
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author Makhloufi, Kahina Maya
Carré-Mlouka, Alyssa
Peduzzi, Jean
Lombard, Carine
van Reenen, Carol Ann
Dicks, Leon Milner Theodore
Rebuffat, Sylvie
author_facet Makhloufi, Kahina Maya
Carré-Mlouka, Alyssa
Peduzzi, Jean
Lombard, Carine
van Reenen, Carol Ann
Dicks, Leon Milner Theodore
Rebuffat, Sylvie
author_sort Makhloufi, Kahina Maya
collection PubMed
description A bacteriocin-producing bacterium was isolated from boza and identified as Leuconostoc pseudomesenteroides KM432Bz. The antimicrobial peptide was purified and shown to be identical to other class IIa bacteriocins: leucocin A from Leuconostoc gelidum UAL-187 and Leuconostoc pseudomesenteroides QU15 and leucocin B from Leuconostoc carnosum Ta11a. The bacteriocin was named leucocin B-KM432Bz. Leucocin B-KM432Bz gene cluster encodes the bacteriocin precursor (lcnB), the immunity protein (lcnI) and the dedicated export machinery (lcnD and lcnE). A gene of unknown and non-essential function (lcnC), which is interrupted by an insertion sequence of the IS30 family, is localized between lcnB and lcnD. The activity of leucocin B-KM432Bz requires subunit C of the EII(t) (Man) mannose permease, which is the receptor for entry into target cells. The determination of the minimum inhibitory concentrations revealed the lowest values for leucocin B-KM432Bz over Listeria strains, with 4 to 32 fold better efficiency than pediocin PA-1.
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spelling pubmed-37312742013-08-09 Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1 Makhloufi, Kahina Maya Carré-Mlouka, Alyssa Peduzzi, Jean Lombard, Carine van Reenen, Carol Ann Dicks, Leon Milner Theodore Rebuffat, Sylvie PLoS One Research Article A bacteriocin-producing bacterium was isolated from boza and identified as Leuconostoc pseudomesenteroides KM432Bz. The antimicrobial peptide was purified and shown to be identical to other class IIa bacteriocins: leucocin A from Leuconostoc gelidum UAL-187 and Leuconostoc pseudomesenteroides QU15 and leucocin B from Leuconostoc carnosum Ta11a. The bacteriocin was named leucocin B-KM432Bz. Leucocin B-KM432Bz gene cluster encodes the bacteriocin precursor (lcnB), the immunity protein (lcnI) and the dedicated export machinery (lcnD and lcnE). A gene of unknown and non-essential function (lcnC), which is interrupted by an insertion sequence of the IS30 family, is localized between lcnB and lcnD. The activity of leucocin B-KM432Bz requires subunit C of the EII(t) (Man) mannose permease, which is the receptor for entry into target cells. The determination of the minimum inhibitory concentrations revealed the lowest values for leucocin B-KM432Bz over Listeria strains, with 4 to 32 fold better efficiency than pediocin PA-1. Public Library of Science 2013-08-01 /pmc/articles/PMC3731274/ /pubmed/23936441 http://dx.doi.org/10.1371/journal.pone.0070484 Text en © 2013 Makhloufi et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Makhloufi, Kahina Maya
Carré-Mlouka, Alyssa
Peduzzi, Jean
Lombard, Carine
van Reenen, Carol Ann
Dicks, Leon Milner Theodore
Rebuffat, Sylvie
Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title_full Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title_fullStr Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title_full_unstemmed Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title_short Characterization of Leucocin B-KM432Bz from Leuconostoc pseudomesenteroides Isolated from Boza, and Comparison of its Efficiency to Pediocin PA-1
title_sort characterization of leucocin b-km432bz from leuconostoc pseudomesenteroides isolated from boza, and comparison of its efficiency to pediocin pa-1
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3731274/
https://www.ncbi.nlm.nih.gov/pubmed/23936441
http://dx.doi.org/10.1371/journal.pone.0070484
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