The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system
In a natural environment, bacteria are members of multispecies communities. To compete with rival species, bacteria produce antimicrobial peptides (AMPs), called bacteriocins. Bacteriocins are small, cationic, ribosomally synthesized peptides, which normally inhibit closely related species of the pr...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-09-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2022.991145/full |
| _version_ | 1828177859447881728 |
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| author | Verena Vogel Lia-Raluca Olari Marie Jachmann Sebastian J. Reich Michelle Häring Ann-Kathrin Kissmann Frank Rosenau Christian U. Riedel Jan Münch Barbara Spellerberg |
| author_facet | Verena Vogel Lia-Raluca Olari Marie Jachmann Sebastian J. Reich Michelle Häring Ann-Kathrin Kissmann Frank Rosenau Christian U. Riedel Jan Münch Barbara Spellerberg |
| author_sort | Verena Vogel |
| collection | DOAJ |
| description | In a natural environment, bacteria are members of multispecies communities. To compete with rival species, bacteria produce antimicrobial peptides (AMPs), called bacteriocins. Bacteriocins are small, cationic, ribosomally synthesized peptides, which normally inhibit closely related species of the producing organism. Bacteriocin production is best studied in lactic bacteria (LAB). Streptococcus anginosus, belonging to LAB, produces the potent bacteriocin Angicin, which shows inhibitory activity against other streptococci, Listeria monocytogenes and vancomycin resistant Enterococcus faecium (VRE). Furthermore, Angicin shows a high resistance toward pH changes and heat, rendering it an interesting candidate for food preservation or clinical applications. The inhibitory activity of Angicin depends on the presence of a mannose phosphotransferase system (Man-PTS) in target cells, since L. monocytogenes harboring a deletion in an extracellular loop of this system is no longer sensitive to Angicin. Furthermore, we demonstrated by liposome leakage and pHluorin assays that Angicin destroys membrane integrity but shows only low cytotoxicity against human cell lines. In conclusion, we show that Angicin has a detrimental effect on the membrane of target organisms by using the Man-PTS as a receptor. |
| first_indexed | 2024-04-12T05:05:10Z |
| format | Article |
| id | doaj.art-baebbe7ca1fe4e45b03654054351ee68 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-12T05:05:10Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-baebbe7ca1fe4e45b03654054351ee682022-12-22T03:46:53ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2022-09-011310.3389/fmicb.2022.991145991145The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase systemVerena Vogel0Lia-Raluca Olari1Marie Jachmann2Sebastian J. Reich3Michelle Häring4Ann-Kathrin Kissmann5Frank Rosenau6Christian U. Riedel7Jan Münch8Barbara Spellerberg9Institute 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, GermanyInstitute of Microbiology and Biotechnology, University of Ulm, Ulm, GermanyInstitute of Pharmaceutical Biotechnology, University of Ulm, Ulm, GermanyInstitute of Pharmaceutical Biotechnology, University of Ulm, Ulm, GermanyInstitute of Pharmaceutical Biotechnology, University of Ulm, Ulm, GermanyInstitute of Microbiology and Biotechnology, University of Ulm, Ulm, GermanyInstitute of Molecular Virology, Ulm University Medical Center, Ulm, GermanyInstitute of Medical Microbiology and Hygiene, Ulm University Medical Center, Ulm, GermanyIn a natural environment, bacteria are members of multispecies communities. To compete with rival species, bacteria produce antimicrobial peptides (AMPs), called bacteriocins. Bacteriocins are small, cationic, ribosomally synthesized peptides, which normally inhibit closely related species of the producing organism. Bacteriocin production is best studied in lactic bacteria (LAB). Streptococcus anginosus, belonging to LAB, produces the potent bacteriocin Angicin, which shows inhibitory activity against other streptococci, Listeria monocytogenes and vancomycin resistant Enterococcus faecium (VRE). Furthermore, Angicin shows a high resistance toward pH changes and heat, rendering it an interesting candidate for food preservation or clinical applications. The inhibitory activity of Angicin depends on the presence of a mannose phosphotransferase system (Man-PTS) in target cells, since L. monocytogenes harboring a deletion in an extracellular loop of this system is no longer sensitive to Angicin. Furthermore, we demonstrated by liposome leakage and pHluorin assays that Angicin destroys membrane integrity but shows only low cytotoxicity against human cell lines. In conclusion, we show that Angicin has a detrimental effect on the membrane of target organisms by using the Man-PTS as a receptor.https://www.frontiersin.org/articles/10.3389/fmicb.2022.991145/fullAngicinStreptococcus anginosusmannose phosphotransferase system (Man-PTS)bacteriocinreceptormode of action (MOA) |
| spellingShingle | Verena Vogel Lia-Raluca Olari Marie Jachmann Sebastian J. Reich Michelle Häring Ann-Kathrin Kissmann Frank Rosenau Christian U. Riedel Jan Münch Barbara Spellerberg The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system Frontiers in Microbiology Angicin Streptococcus anginosus mannose phosphotransferase system (Man-PTS) bacteriocin receptor mode of action (MOA) |
| title | The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| title_full | The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| title_fullStr | The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| title_full_unstemmed | The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| title_short | The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| title_sort | bacteriocin angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system |
| topic | Angicin Streptococcus anginosus mannose phosphotransferase system (Man-PTS) bacteriocin receptor mode of action (MOA) |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2022.991145/full |
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