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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...

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Autores principales: Vogel, Verena, Fuchs, Miki, Jachmann, Marie, Bitzer, Alina, Mauerer, Stefanie, Münch, Jan, Spellerberg, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
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.
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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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