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Garvicin Q: characterization of biosynthesis and mode of action
Bacteriocins are ribosomally synthesized antimicrobial peptides, that either kill target bacteria or inhibit their growth. Bacteriocins are used in food preservation and are of increasing interest as potential alternatives to conventional antibiotics. In the present study, we show that Lactococcus p...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9652874/ https://www.ncbi.nlm.nih.gov/pubmed/36368990 http://dx.doi.org/10.1186/s12934-022-01952-9 |
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author | Desiderato, Christian K. Hasenauer, Katharina M. Reich, Sebastian J. Goldbeck, Oliver Holivololona, Lalaina Ovchinnikov, Kirill V. Reiter, Alexander Oldiges, Marco Diep, Dzung B. Eikmanns, Bernhard J. Riedel, Christian U. |
author_facet | Desiderato, Christian K. Hasenauer, Katharina M. Reich, Sebastian J. Goldbeck, Oliver Holivololona, Lalaina Ovchinnikov, Kirill V. Reiter, Alexander Oldiges, Marco Diep, Dzung B. Eikmanns, Bernhard J. Riedel, Christian U. |
author_sort | Desiderato, Christian K. |
collection | PubMed |
description | Bacteriocins are ribosomally synthesized antimicrobial peptides, that either kill target bacteria or inhibit their growth. Bacteriocins are used in food preservation and are of increasing interest as potential alternatives to conventional antibiotics. In the present study, we show that Lactococcus petauri B1726, a strain isolated from fermented balsam pear, produces a heat-stable and protease-sensitive compound. Following genome sequencing, a gene cluster for production of a class IId bacteriocin was identified consisting of garQ (encoding for the bacteriocin garvicin Q), garI (for a putative immunity protein), garC, and garD (putative transporter proteins). Growth conditions were optimized for increased bacteriocin activity in supernatants of L. petauri B1726 and purification and mass spectrometry identified the compound as garvicin Q. Further experiments suggest that garvicin Q adsorbs to biomass of various susceptible and insusceptible bacteria and support the hypothesis that garvicin Q requires a mannose-family phosphotransferase system (PTS(Man)) as receptor to kill target bacteria by disruption of membrane integrity. Heterologous expression of a synthetic garQICD operon was established in Corynebacterium glutamicum demonstrating that genes garQICD are responsible for biosynthesis and secretion of garvicin Q. Moreover, production of garvicin Q by the recombinant C. glutamicum strain was improved by using a defined medium yet product levels were still considerably lower than with the natural L. petauri B1726 producer strain. Collectively, our data identifies the genetic basis for production of the bacteriocin garvicin Q by L. petauri B1726 and provides insights into the receptor and mode of action of garvicin Q. Moreover, we successfully performed first attempts towards biotechnological production of this interesting bacteriocin using natural and heterologous hosts. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12934-022-01952-9. |
format | Online Article Text |
id | pubmed-9652874 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-96528742022-11-15 Garvicin Q: characterization of biosynthesis and mode of action Desiderato, Christian K. Hasenauer, Katharina M. Reich, Sebastian J. Goldbeck, Oliver Holivololona, Lalaina Ovchinnikov, Kirill V. Reiter, Alexander Oldiges, Marco Diep, Dzung B. Eikmanns, Bernhard J. Riedel, Christian U. Microb Cell Fact Research Bacteriocins are ribosomally synthesized antimicrobial peptides, that either kill target bacteria or inhibit their growth. Bacteriocins are used in food preservation and are of increasing interest as potential alternatives to conventional antibiotics. In the present study, we show that Lactococcus petauri B1726, a strain isolated from fermented balsam pear, produces a heat-stable and protease-sensitive compound. Following genome sequencing, a gene cluster for production of a class IId bacteriocin was identified consisting of garQ (encoding for the bacteriocin garvicin Q), garI (for a putative immunity protein), garC, and garD (putative transporter proteins). Growth conditions were optimized for increased bacteriocin activity in supernatants of L. petauri B1726 and purification and mass spectrometry identified the compound as garvicin Q. Further experiments suggest that garvicin Q adsorbs to biomass of various susceptible and insusceptible bacteria and support the hypothesis that garvicin Q requires a mannose-family phosphotransferase system (PTS(Man)) as receptor to kill target bacteria by disruption of membrane integrity. Heterologous expression of a synthetic garQICD operon was established in Corynebacterium glutamicum demonstrating that genes garQICD are responsible for biosynthesis and secretion of garvicin Q. Moreover, production of garvicin Q by the recombinant C. glutamicum strain was improved by using a defined medium yet product levels were still considerably lower than with the natural L. petauri B1726 producer strain. Collectively, our data identifies the genetic basis for production of the bacteriocin garvicin Q by L. petauri B1726 and provides insights into the receptor and mode of action of garvicin Q. Moreover, we successfully performed first attempts towards biotechnological production of this interesting bacteriocin using natural and heterologous hosts. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12934-022-01952-9. BioMed Central 2022-11-11 /pmc/articles/PMC9652874/ /pubmed/36368990 http://dx.doi.org/10.1186/s12934-022-01952-9 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis 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/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Desiderato, Christian K. Hasenauer, Katharina M. Reich, Sebastian J. Goldbeck, Oliver Holivololona, Lalaina Ovchinnikov, Kirill V. Reiter, Alexander Oldiges, Marco Diep, Dzung B. Eikmanns, Bernhard J. Riedel, Christian U. Garvicin Q: characterization of biosynthesis and mode of action |
title | Garvicin Q: characterization of biosynthesis and mode of action |
title_full | Garvicin Q: characterization of biosynthesis and mode of action |
title_fullStr | Garvicin Q: characterization of biosynthesis and mode of action |
title_full_unstemmed | Garvicin Q: characterization of biosynthesis and mode of action |
title_short | Garvicin Q: characterization of biosynthesis and mode of action |
title_sort | garvicin q: characterization of biosynthesis and mode of action |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9652874/ https://www.ncbi.nlm.nih.gov/pubmed/36368990 http://dx.doi.org/10.1186/s12934-022-01952-9 |
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