Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk
Biosurfactants such as lipopeptides are amphiphilic compounds produced by microorganisms such as bacteria of the genera of Pseudomonas and Bacillus. Some of these molecules proved to have interesting antimicrobial, antiviral, insecticide and/or tensio-active properties that are potentially useful fo...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2018-05-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2018.01030/full |
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| author | Margot Schlusselhuber Justine Godard Muriel Sebban Benoit Bernay David Garon Virginie Seguin Hassan Oulyadi Nathalie Desmasures |
| author_facet | Margot Schlusselhuber Justine Godard Muriel Sebban Benoit Bernay David Garon Virginie Seguin Hassan Oulyadi Nathalie Desmasures |
| author_sort | Margot Schlusselhuber |
| collection | DOAJ |
| description | Biosurfactants such as lipopeptides are amphiphilic compounds produced by microorganisms such as bacteria of the genera of Pseudomonas and Bacillus. Some of these molecules proved to have interesting antimicrobial, antiviral, insecticide and/or tensio-active properties that are potentially useful for the agricultural, chemical, food, and pharmaceutical industries. Raw milk provides a physicochemical environment that is favorable to the multiplication of a broad spectrum of microorganisms. Among them, psychrotrophic bacterial species, especially members of the genus Pseudomonas, are predominant and colonize milk during cold storage and/or processing. We isolated the strain Pseudomonas sp. UCMA 17988 from raw cow milk, with antagonistic activity against Listeria monocytogenes, Staphylococcus aureus, and Salmonella enterica Newport. Antimicrobial molecules involved in the antagonistic activity of this strain were characterized. A mass spectrometry analysis highlighted the presence of four lipopeptides isoforms. The major isoform (1409 m/z), composed of 10 carbons in the lipidic chain, was named milkisin C. The three other isoforms detected at 1381, 1395, and 1423 m/z, that are concomitantly produced, were named milkisin A, B and D, respectively. The structure of milkisin, as confirmed by NMR analyses, is closely related to amphisin family. Indeed, the peptidic chain was composed of 11 amino acids, 9 of which are conserved among the family. In conclusion, Pseudomonas sp. UCMA 17988 produces new members of the amphisin family which are responsible for the antagonistic activity of this strain. |
| first_indexed | 2024-04-13T09:57:28Z |
| format | Article |
| id | doaj.art-52b92dc8010048a7af991890bc7db3c1 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-13T09:57:28Z |
| publishDate | 2018-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-52b92dc8010048a7af991890bc7db3c12022-12-22T02:51:19ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2018-05-01910.3389/fmicb.2018.01030355822Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw MilkMargot Schlusselhuber0Justine Godard1Muriel Sebban2Benoit Bernay3David Garon4Virginie Seguin5Hassan Oulyadi6Nathalie Desmasures7UNICAEN, UNIROUEN, ABTE, Normandie Université, Caen, FranceUNICAEN, UNIROUEN, ABTE, Normandie Université, Caen, FranceUNIROUEN, INSA Rouen, CNRS, COBRA, Normandie Université, Rouen, FranceUNICAEN, SF ICORE 4206, Normandie Université, Caen, FranceUNICAEN, UNIROUEN, ABTE, Normandie Université, Caen, FranceUNICAEN, UNIROUEN, ABTE, Normandie Université, Caen, FranceUNIROUEN, INSA Rouen, CNRS, COBRA, Normandie Université, Rouen, FranceUNICAEN, UNIROUEN, ABTE, Normandie Université, Caen, FranceBiosurfactants such as lipopeptides are amphiphilic compounds produced by microorganisms such as bacteria of the genera of Pseudomonas and Bacillus. Some of these molecules proved to have interesting antimicrobial, antiviral, insecticide and/or tensio-active properties that are potentially useful for the agricultural, chemical, food, and pharmaceutical industries. Raw milk provides a physicochemical environment that is favorable to the multiplication of a broad spectrum of microorganisms. Among them, psychrotrophic bacterial species, especially members of the genus Pseudomonas, are predominant and colonize milk during cold storage and/or processing. We isolated the strain Pseudomonas sp. UCMA 17988 from raw cow milk, with antagonistic activity against Listeria monocytogenes, Staphylococcus aureus, and Salmonella enterica Newport. Antimicrobial molecules involved in the antagonistic activity of this strain were characterized. A mass spectrometry analysis highlighted the presence of four lipopeptides isoforms. The major isoform (1409 m/z), composed of 10 carbons in the lipidic chain, was named milkisin C. The three other isoforms detected at 1381, 1395, and 1423 m/z, that are concomitantly produced, were named milkisin A, B and D, respectively. The structure of milkisin, as confirmed by NMR analyses, is closely related to amphisin family. Indeed, the peptidic chain was composed of 11 amino acids, 9 of which are conserved among the family. In conclusion, Pseudomonas sp. UCMA 17988 produces new members of the amphisin family which are responsible for the antagonistic activity of this strain.https://www.frontiersin.org/article/10.3389/fmicb.2018.01030/fullantimicrobial activityPseudomonasmilkisinamphisinlipopeptide |
| spellingShingle | Margot Schlusselhuber Justine Godard Muriel Sebban Benoit Bernay David Garon Virginie Seguin Hassan Oulyadi Nathalie Desmasures Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk Frontiers in Microbiology antimicrobial activity Pseudomonas milkisin amphisin lipopeptide |
| title | Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk |
| title_full | Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk |
| title_fullStr | Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk |
| title_full_unstemmed | Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk |
| title_short | Characterization of Milkisin, a Novel Lipopeptide With Antimicrobial Properties Produced By Pseudomonas sp. UCMA 17988 Isolated From Bovine Raw Milk |
| title_sort | characterization of milkisin a novel lipopeptide with antimicrobial properties produced by pseudomonas sp ucma 17988 isolated from bovine raw milk |
| topic | antimicrobial activity Pseudomonas milkisin amphisin lipopeptide |
| url | https://www.frontiersin.org/article/10.3389/fmicb.2018.01030/full |
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