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Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin

Bacteriocins are antibacterial, proteinaceous substances that mediate microbial dynamics. Bacteriocin production is a highly disseminated property among all major lineages of bacteria, including Shigella. In this paper, we addressed the purification and characterisation of a bacteriocin produced by...

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Autores principales: Sousa, Mireille Ângela Bernardes, Farias, Luiz de Macêdo, de Oliveira, Patrícia Luciana, Moreira, Jaqueline Silvana, Apolônio, Ana Carolina Morais, Oliveira, Jamil Silvano, Santoro, Marcelo Matos, Mendes, Edilberto Nogueira, Magalhães, Paula Prazeres
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Instituto Oswaldo Cruz, Ministério da Saúde 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970690/
https://www.ncbi.nlm.nih.gov/pubmed/24037194
http://dx.doi.org/10.1590/0074-0276108062013008
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author Sousa, Mireille Ângela Bernardes
Farias, Luiz de Macêdo
de Oliveira, Patrícia Luciana
Moreira, Jaqueline Silvana
Apolônio, Ana Carolina Morais
Oliveira, Jamil Silvano
Santoro, Marcelo Matos
Mendes, Edilberto Nogueira
Magalhães, Paula Prazeres
author_facet Sousa, Mireille Ângela Bernardes
Farias, Luiz de Macêdo
de Oliveira, Patrícia Luciana
Moreira, Jaqueline Silvana
Apolônio, Ana Carolina Morais
Oliveira, Jamil Silvano
Santoro, Marcelo Matos
Mendes, Edilberto Nogueira
Magalhães, Paula Prazeres
author_sort Sousa, Mireille Ângela Bernardes
collection PubMed
description Bacteriocins are antibacterial, proteinaceous substances that mediate microbial dynamics. Bacteriocin production is a highly disseminated property among all major lineages of bacteria, including Shigella. In this paper, we addressed the purification and characterisation of a bacteriocin produced by a Shigella sonnei strain (SS9) isolated from a child with acute diarrhoea. The substance was purified through ammonium-sulphate precipitation and sequential steps of chromatography. The intracellular fraction obtained at 75% ammonium sulphate maintained activity following exposure to pH values from 1-11 and storage at -80ºC for more than two years and was inactivated by high temperatures and proteases. The molecular mass of the purified bacteriocin was determined by mass spectrometry to be 18.56 kDa. The N-terminal sequence of the bacteriocin did not match any other antibacterial proteins described. A putative new bacteriocin produced by S. sonnei has been detected. This bacteriocin may represent a newly described protein or a previously described protein with a newly detected function. Considering that SS9 expresses antagonism against other diarrhoeagenic bacteria, the bacteriocin may contribute to S. sonnei virulence and is potentially applicable to either preventing or controlling diarrhoeal disease.
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spelling pubmed-39706902014-05-21 Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin Sousa, Mireille Ângela Bernardes Farias, Luiz de Macêdo de Oliveira, Patrícia Luciana Moreira, Jaqueline Silvana Apolônio, Ana Carolina Morais Oliveira, Jamil Silvano Santoro, Marcelo Matos Mendes, Edilberto Nogueira Magalhães, Paula Prazeres Mem Inst Oswaldo Cruz Articles Bacteriocins are antibacterial, proteinaceous substances that mediate microbial dynamics. Bacteriocin production is a highly disseminated property among all major lineages of bacteria, including Shigella. In this paper, we addressed the purification and characterisation of a bacteriocin produced by a Shigella sonnei strain (SS9) isolated from a child with acute diarrhoea. The substance was purified through ammonium-sulphate precipitation and sequential steps of chromatography. The intracellular fraction obtained at 75% ammonium sulphate maintained activity following exposure to pH values from 1-11 and storage at -80ºC for more than two years and was inactivated by high temperatures and proteases. The molecular mass of the purified bacteriocin was determined by mass spectrometry to be 18.56 kDa. The N-terminal sequence of the bacteriocin did not match any other antibacterial proteins described. A putative new bacteriocin produced by S. sonnei has been detected. This bacteriocin may represent a newly described protein or a previously described protein with a newly detected function. Considering that SS9 expresses antagonism against other diarrhoeagenic bacteria, the bacteriocin may contribute to S. sonnei virulence and is potentially applicable to either preventing or controlling diarrhoeal disease. Instituto Oswaldo Cruz, Ministério da Saúde 2013-09 /pmc/articles/PMC3970690/ /pubmed/24037194 http://dx.doi.org/10.1590/0074-0276108062013008 Text en http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Sousa, Mireille Ângela Bernardes
Farias, Luiz de Macêdo
de Oliveira, Patrícia Luciana
Moreira, Jaqueline Silvana
Apolônio, Ana Carolina Morais
Oliveira, Jamil Silvano
Santoro, Marcelo Matos
Mendes, Edilberto Nogueira
Magalhães, Paula Prazeres
Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title_full Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title_fullStr Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title_full_unstemmed Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title_short Antagonistic activity expressed by Shigella sonnei: identification of a putative new bacteriocin
title_sort antagonistic activity expressed by shigella sonnei: identification of a putative new bacteriocin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970690/
https://www.ncbi.nlm.nih.gov/pubmed/24037194
http://dx.doi.org/10.1590/0074-0276108062013008
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