Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3
Genome mining has emerged as a revolutionary tool for discovering new ribosomally synthesized and post-translationally modified peptides (RiPPs) in various genomes. Recently, these approaches have been used to detect and explore unique environments as sources of RiPP-producing microorganisms, partic...
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| Format: | Article |
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MDPI AG
2024-12-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/13/12/1179 |
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| author | Dora Onely Roblero-Mejía Carlos García-Ausencio Romina Rodríguez-Sanoja Fernando Guzmán-Chávez Sergio Sánchez |
| author_facet | Dora Onely Roblero-Mejía Carlos García-Ausencio Romina Rodríguez-Sanoja Fernando Guzmán-Chávez Sergio Sánchez |
| author_sort | Dora Onely Roblero-Mejía |
| collection | DOAJ |
| description | Genome mining has emerged as a revolutionary tool for discovering new ribosomally synthesized and post-translationally modified peptides (RiPPs) in various genomes. Recently, these approaches have been used to detect and explore unique environments as sources of RiPP-producing microorganisms, particularly focusing on endophytic microorganisms found in medicinal plants. Some endophytic actinobacteria, especially strains of <i>Streptomyces</i>, are notable examples of peptide producers, as specific biosynthetic clusters encode them. To uncover the genetic potential of these organisms, we analyzed the genome of the endophytic actinobacterium <i>Embleya</i> sp. NF3 using genome mining and bioinformatics tools. Our analysis led to the identification of a putative class I lanthipeptide. We cloned the core biosynthetic genes of this putative lanthipeptide, named embleporicin, and expressed them in vitro using a cell-free protein system (CFPS). The resulting product demonstrated antimicrobial activity against <i>Micrococcus luteus</i> ATCC 9341. This represents the first RiPP reported in the genus <i>Embleya</i> and the first actinobacterial lanthipeptide produced through cell-free technology. |
| format | Article |
| id | doaj-art-745ef93add4b4ce18bbbe8c169ae13c7 |
| institution | Kabale University |
| issn | 2079-6382 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj-art-745ef93add4b4ce18bbbe8c169ae13c72024-12-27T14:06:17ZengMDPI AGAntibiotics2079-63822024-12-011312117910.3390/antibiotics13121179Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3Dora Onely Roblero-Mejía0Carlos García-Ausencio1Romina Rodríguez-Sanoja2Fernando Guzmán-Chávez3Sergio Sánchez4Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City 04510, MexicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City 04510, MexicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City 04510, MexicoDepartamento de Alimentos y Biotecnología, Facultad de Química, Universidad Nacional Autónoma de México (UNAM), Mexico City 04510, MexicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), Mexico City 04510, MexicoGenome mining has emerged as a revolutionary tool for discovering new ribosomally synthesized and post-translationally modified peptides (RiPPs) in various genomes. Recently, these approaches have been used to detect and explore unique environments as sources of RiPP-producing microorganisms, particularly focusing on endophytic microorganisms found in medicinal plants. Some endophytic actinobacteria, especially strains of <i>Streptomyces</i>, are notable examples of peptide producers, as specific biosynthetic clusters encode them. To uncover the genetic potential of these organisms, we analyzed the genome of the endophytic actinobacterium <i>Embleya</i> sp. NF3 using genome mining and bioinformatics tools. Our analysis led to the identification of a putative class I lanthipeptide. We cloned the core biosynthetic genes of this putative lanthipeptide, named embleporicin, and expressed them in vitro using a cell-free protein system (CFPS). The resulting product demonstrated antimicrobial activity against <i>Micrococcus luteus</i> ATCC 9341. This represents the first RiPP reported in the genus <i>Embleya</i> and the first actinobacterial lanthipeptide produced through cell-free technology.https://www.mdpi.com/2079-6382/13/12/1179actinobacterium <i>Embleya</i> sp. NF3genome mininglanthipeptidesantimicrobialscell-free expression |
| spellingShingle | Dora Onely Roblero-Mejía Carlos García-Ausencio Romina Rodríguez-Sanoja Fernando Guzmán-Chávez Sergio Sánchez Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 Antibiotics actinobacterium <i>Embleya</i> sp. NF3 genome mining lanthipeptides antimicrobials cell-free expression |
| title | Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 |
| title_full | Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 |
| title_fullStr | Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 |
| title_full_unstemmed | Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 |
| title_short | Embleporicin: A Novel Class I Lanthipeptide from the Actinobacteria <i>Embleya</i> sp. NF3 |
| title_sort | embleporicin a novel class i lanthipeptide from the actinobacteria i embleya i sp nf3 |
| topic | actinobacterium <i>Embleya</i> sp. NF3 genome mining lanthipeptides antimicrobials cell-free expression |
| url | https://www.mdpi.com/2079-6382/13/12/1179 |
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