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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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2022-07-01
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Series: | Frontiers in Microbiology |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2022.904318/full |
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author | Verena Vogel Miki Fuchs Marie Jachmann Alina Bitzer Stefanie Mauerer Jan Münch Barbara Spellerberg |
author_facet | Verena Vogel Miki Fuchs Marie Jachmann Alina Bitzer Stefanie Mauerer Jan Münch Barbara Spellerberg |
author_sort | Verena Vogel |
collection | DOAJ |
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. |
first_indexed | 2024-04-13T11:46:05Z |
format | Article |
id | doaj.art-7c12551955174422aade7056b6b42008 |
institution | Directory Open Access Journal |
issn | 1664-302X |
language | English |
last_indexed | 2024-04-13T11:46:05Z |
publishDate | 2022-07-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Microbiology |
spelling | doaj.art-7c12551955174422aade7056b6b420082022-12-22T02:48:10ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2022-07-011310.3389/fmicb.2022.904318904318The Role of SilX in Bacteriocin Production of Streptococcus anginosusVerena Vogel0Miki Fuchs1Marie Jachmann2Alina Bitzer3Stefanie Mauerer4Jan Münch5Barbara Spellerberg6Institute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyInstitute of Molecular Virology, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyStreptococcus 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.https://www.frontiersin.org/articles/10.3389/fmicb.2022.904318/fullStreptococcus anginosusCAAX proteasebacteriocinAngicinstreptococcal invasion locusHIV protease inhibitor |
spellingShingle | Verena Vogel Miki Fuchs Marie Jachmann Alina Bitzer Stefanie Mauerer Jan Münch Barbara Spellerberg The Role of SilX in Bacteriocin Production of Streptococcus anginosus Frontiers in Microbiology Streptococcus anginosus CAAX protease bacteriocin Angicin streptococcal invasion locus HIV protease inhibitor |
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 | Streptococcus anginosus CAAX protease bacteriocin Angicin streptococcal invasion locus HIV protease inhibitor |
url | https://www.frontiersin.org/articles/10.3389/fmicb.2022.904318/full |
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