Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein
Abstract Lactic acid bacteria produce a variety of antimicrobial peptides known as bacteriocins. Most bacteriocins are understood to kill sensitive bacteria through receptor‐mediated disruptions. Here, we report on the identification of the Lactobacillus plantarum plantaricin EF (PlnEF) receptor. Sp...
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| Format: | Article |
| Language: | English |
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Wiley
2019-11-01
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| Series: | MicrobiologyOpen |
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| Online Access: | https://doi.org/10.1002/mbo3.827 |
| _version_ | 1828366473518645248 |
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| author | Dustin D. Heeney Vladimir Yarov‐Yarovoy Maria L. Marco |
| author_facet | Dustin D. Heeney Vladimir Yarov‐Yarovoy Maria L. Marco |
| author_sort | Dustin D. Heeney |
| collection | DOAJ |
| description | Abstract Lactic acid bacteria produce a variety of antimicrobial peptides known as bacteriocins. Most bacteriocins are understood to kill sensitive bacteria through receptor‐mediated disruptions. Here, we report on the identification of the Lactobacillus plantarum plantaricin EF (PlnEF) receptor. Spontaneous PlnEF‐resistant mutants of the PlnEF‐indicator strain L. plantarum NCIMB 700965 (LP965) were isolated and confirmed to maintain cellular ATP levels in the presence of PlnEF. Genome comparisons resulted in the identification of a single mutated gene annotated as the membrane‐bound, magnesium/cobalt efflux protein CorC. All isolates contained a valine (V) at position 334 instead of a glycine (G) in a cysteine‐β‐synthase domain at the C‐terminal region of CorC. In silico template‐based modeling of this domain indicated that the mutation resides in a loop between two β‐strands. The relationship between PlnEF, CorC, and metal homeostasis was supported by the finding that PlnEF‐resistance was lost when PlnEF was applied together with high concentrations of Mg2+, Co2+, Zn2+, or Cu2+. Lastly, PlnEF sensitivity was increased upon heterologous expression of LP965 corC but not the G334V CorC mutant in the PlnEF‐resistant strain Lactobacillus casei BL23. These results show that PlnEF kills sensitive bacteria by targeting CorC. |
| first_indexed | 2024-04-14T05:46:28Z |
| format | Article |
| id | doaj.art-28acb69f442f401a91ba59f6a3a89cc0 |
| institution | Directory Open Access Journal |
| issn | 2045-8827 |
| language | English |
| last_indexed | 2024-04-14T05:46:28Z |
| publishDate | 2019-11-01 |
| publisher | Wiley |
| record_format | Article |
| series | MicrobiologyOpen |
| spelling | doaj.art-28acb69f442f401a91ba59f6a3a89cc02022-12-22T02:09:17ZengWileyMicrobiologyOpen2045-88272019-11-01811n/an/a10.1002/mbo3.827Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux proteinDustin D. Heeney0Vladimir Yarov‐Yarovoy1Maria L. Marco2Department of Food Science & Technology University of California‐Davis Davis CaliforniaDepartment of Physiology and Membrane Biology University of California‐Davis Davis CaliforniaDepartment of Food Science & Technology University of California‐Davis Davis CaliforniaAbstract Lactic acid bacteria produce a variety of antimicrobial peptides known as bacteriocins. Most bacteriocins are understood to kill sensitive bacteria through receptor‐mediated disruptions. Here, we report on the identification of the Lactobacillus plantarum plantaricin EF (PlnEF) receptor. Spontaneous PlnEF‐resistant mutants of the PlnEF‐indicator strain L. plantarum NCIMB 700965 (LP965) were isolated and confirmed to maintain cellular ATP levels in the presence of PlnEF. Genome comparisons resulted in the identification of a single mutated gene annotated as the membrane‐bound, magnesium/cobalt efflux protein CorC. All isolates contained a valine (V) at position 334 instead of a glycine (G) in a cysteine‐β‐synthase domain at the C‐terminal region of CorC. In silico template‐based modeling of this domain indicated that the mutation resides in a loop between two β‐strands. The relationship between PlnEF, CorC, and metal homeostasis was supported by the finding that PlnEF‐resistance was lost when PlnEF was applied together with high concentrations of Mg2+, Co2+, Zn2+, or Cu2+. Lastly, PlnEF sensitivity was increased upon heterologous expression of LP965 corC but not the G334V CorC mutant in the PlnEF‐resistant strain Lactobacillus casei BL23. These results show that PlnEF kills sensitive bacteria by targeting CorC.https://doi.org/10.1002/mbo3.827antimicrobial resistancebacteriocinslactic acid bacteriaLactobacillusprobiotics |
| spellingShingle | Dustin D. Heeney Vladimir Yarov‐Yarovoy Maria L. Marco Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein MicrobiologyOpen antimicrobial resistance bacteriocins lactic acid bacteria Lactobacillus probiotics |
| title | Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein |
| title_full | Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein |
| title_fullStr | Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein |
| title_full_unstemmed | Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein |
| title_short | Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein |
| title_sort | sensitivity to the two peptide bacteriocin plantaricin ef is dependent on corc a membrane bound magnesium cobalt efflux protein |
| topic | antimicrobial resistance bacteriocins lactic acid bacteria Lactobacillus probiotics |
| url | https://doi.org/10.1002/mbo3.827 |
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