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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Instituto Oswaldo Cruz, Ministério da Saúde
2013
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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. |
format | Online Article Text |
id | pubmed-3970690 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Instituto Oswaldo Cruz, Ministério da Saúde |
record_format | MEDLINE/PubMed |
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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