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The Role of SilX in Bacteriocin Production of Streptococcus anginosus
Streptococcus anginosus produces the novel antimicrobial peptide Angicin, which inhibits Gram positive microorganisms and is classified as a group IId bacteriocin. Production of Angicin is regulated by the quorum sensing system Sil (Streptococcus invasion locus), which is located adjacent to the bac...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9298176/ https://www.ncbi.nlm.nih.gov/pubmed/35875552 http://dx.doi.org/10.3389/fmicb.2022.904318 |
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author | Vogel, Verena Fuchs, Miki Jachmann, Marie Bitzer, Alina Mauerer, Stefanie Münch, Jan Spellerberg, Barbara |
author_facet | Vogel, Verena Fuchs, Miki Jachmann, Marie Bitzer, Alina Mauerer, Stefanie Münch, Jan Spellerberg, Barbara |
author_sort | Vogel, Verena |
collection | PubMed |
description | Streptococcus anginosus produces the novel antimicrobial peptide Angicin, which inhibits Gram positive microorganisms and is classified as a group IId bacteriocin. Production of Angicin is regulated by the quorum sensing system Sil (Streptococcus invasion locus), which is located adjacent to the bacteriocin gene cluster. Within this genetic region a typical CAAX protease is encoded, which was designated SilX. Nelfinavir, a HIV protease inhibitor, led to a concentration dependent reduction in antimicrobial activity, presumably through the inhibition of SilX. Concentrations exceeding 25 μM Nelfinavir caused a complete abolishment of bacteriocin activity against Listeria monocytogenes. These results are supported by the observation, that a SilX deletion mutant of S. anginosus strain BSU 1211 no longer inhibits the growth of L. monocytogenes. Antimicrobial activity could be restored by addition of synthetically synthesized mature SilCR, implying that SilX may be involved in the export and processing of the signal peptide SilCR. Some CAAX proteases have been reported to provide immunity against bacteriocins. However, in a radial diffusion assay the deletion mutant S. anginosus BSU 1211ΔSilX showed no sensitivity toward Angicin arguing against a role of SilX in the immunity of S. anginosus. The putative processing of the signal peptide SilCR indicates a novel function of the CAAX protease SilX, in the context of S. anginosus bacteriocin production. |
format | Online Article Text |
id | pubmed-9298176 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92981762022-07-21 The Role of SilX in Bacteriocin Production of Streptococcus anginosus Vogel, Verena Fuchs, Miki Jachmann, Marie Bitzer, Alina Mauerer, Stefanie Münch, Jan Spellerberg, Barbara Front Microbiol Microbiology Streptococcus anginosus produces the novel antimicrobial peptide Angicin, which inhibits Gram positive microorganisms and is classified as a group IId bacteriocin. Production of Angicin is regulated by the quorum sensing system Sil (Streptococcus invasion locus), which is located adjacent to the bacteriocin gene cluster. Within this genetic region a typical CAAX protease is encoded, which was designated SilX. Nelfinavir, a HIV protease inhibitor, led to a concentration dependent reduction in antimicrobial activity, presumably through the inhibition of SilX. Concentrations exceeding 25 μM Nelfinavir caused a complete abolishment of bacteriocin activity against Listeria monocytogenes. These results are supported by the observation, that a SilX deletion mutant of S. anginosus strain BSU 1211 no longer inhibits the growth of L. monocytogenes. Antimicrobial activity could be restored by addition of synthetically synthesized mature SilCR, implying that SilX may be involved in the export and processing of the signal peptide SilCR. Some CAAX proteases have been reported to provide immunity against bacteriocins. However, in a radial diffusion assay the deletion mutant S. anginosus BSU 1211ΔSilX showed no sensitivity toward Angicin arguing against a role of SilX in the immunity of S. anginosus. The putative processing of the signal peptide SilCR indicates a novel function of the CAAX protease SilX, in the context of S. anginosus bacteriocin production. Frontiers Media S.A. 2022-07-01 /pmc/articles/PMC9298176/ /pubmed/35875552 http://dx.doi.org/10.3389/fmicb.2022.904318 Text en Copyright © 2022 Vogel, Fuchs, Jachmann, Bitzer, Mauerer, Münch and Spellerberg. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Vogel, Verena Fuchs, Miki Jachmann, Marie Bitzer, Alina Mauerer, Stefanie Münch, Jan Spellerberg, Barbara The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title | The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title_full | The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title_fullStr | The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title_full_unstemmed | The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title_short | The Role of SilX in Bacteriocin Production of Streptococcus anginosus |
title_sort | role of silx in bacteriocin production of streptococcus anginosus |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9298176/ https://www.ncbi.nlm.nih.gov/pubmed/35875552 http://dx.doi.org/10.3389/fmicb.2022.904318 |
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