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Angicin, a novel bacteriocin of Streptococcus anginosus
As a conserved defense mechanism, many bacteria produce antimicrobial peptides, called bacteriocins, which provide a colonization advantage in a multispecies environment. Here the first bacteriocin of Streptococcus anginosus, designated Angicin, is described. S. anginosus is commonly described as a...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8692603/ https://www.ncbi.nlm.nih.gov/pubmed/34934110 http://dx.doi.org/10.1038/s41598-021-03797-5 |
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author | Vogel, Verena Bauer, Richard Mauerer, Stefanie Schiffelholz, Nicole Haupt, Christian Seibold, Gerd M. Fändrich, Marcus Walther, Paul Spellerberg, Barbara |
author_facet | Vogel, Verena Bauer, Richard Mauerer, Stefanie Schiffelholz, Nicole Haupt, Christian Seibold, Gerd M. Fändrich, Marcus Walther, Paul Spellerberg, Barbara |
author_sort | Vogel, Verena |
collection | PubMed |
description | As a conserved defense mechanism, many bacteria produce antimicrobial peptides, called bacteriocins, which provide a colonization advantage in a multispecies environment. Here the first bacteriocin of Streptococcus anginosus, designated Angicin, is described. S. anginosus is commonly described as a commensal, however it also possesses a high pathogenic potential. Therefore, understanding factors contributing to its host colonization and persistence are important. A radial diffusion assay was used to identify S. anginosus BSU 1211 as a potent bacteriocin producer. By genetic mutagenesis the background of bacteriocin production and the bacteriocin gene itself were identified. Synthetic Angicin shows high activity against closely related streptococci, listeria and vancomycin resistant enterococci. It has a fast mechanism of action and causes a membrane disruption in target cells. Angicin, present in cell free supernatant, is insensitive to changes in temperature from − 70 to 90 °C and pH values from 2 to 10, suggesting that it represents an interesting compound for potential applications in food preservation or clinical settings. |
format | Online Article Text |
id | pubmed-8692603 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-86926032021-12-28 Angicin, a novel bacteriocin of Streptococcus anginosus Vogel, Verena Bauer, Richard Mauerer, Stefanie Schiffelholz, Nicole Haupt, Christian Seibold, Gerd M. Fändrich, Marcus Walther, Paul Spellerberg, Barbara Sci Rep Article As a conserved defense mechanism, many bacteria produce antimicrobial peptides, called bacteriocins, which provide a colonization advantage in a multispecies environment. Here the first bacteriocin of Streptococcus anginosus, designated Angicin, is described. S. anginosus is commonly described as a commensal, however it also possesses a high pathogenic potential. Therefore, understanding factors contributing to its host colonization and persistence are important. A radial diffusion assay was used to identify S. anginosus BSU 1211 as a potent bacteriocin producer. By genetic mutagenesis the background of bacteriocin production and the bacteriocin gene itself were identified. Synthetic Angicin shows high activity against closely related streptococci, listeria and vancomycin resistant enterococci. It has a fast mechanism of action and causes a membrane disruption in target cells. Angicin, present in cell free supernatant, is insensitive to changes in temperature from − 70 to 90 °C and pH values from 2 to 10, suggesting that it represents an interesting compound for potential applications in food preservation or clinical settings. Nature Publishing Group UK 2021-12-21 /pmc/articles/PMC8692603/ /pubmed/34934110 http://dx.doi.org/10.1038/s41598-021-03797-5 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Vogel, Verena Bauer, Richard Mauerer, Stefanie Schiffelholz, Nicole Haupt, Christian Seibold, Gerd M. Fändrich, Marcus Walther, Paul Spellerberg, Barbara Angicin, a novel bacteriocin of Streptococcus anginosus |
title | Angicin, a novel bacteriocin of Streptococcus anginosus |
title_full | Angicin, a novel bacteriocin of Streptococcus anginosus |
title_fullStr | Angicin, a novel bacteriocin of Streptococcus anginosus |
title_full_unstemmed | Angicin, a novel bacteriocin of Streptococcus anginosus |
title_short | Angicin, a novel bacteriocin of Streptococcus anginosus |
title_sort | angicin, a novel bacteriocin of streptococcus anginosus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8692603/ https://www.ncbi.nlm.nih.gov/pubmed/34934110 http://dx.doi.org/10.1038/s41598-021-03797-5 |
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