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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Main Authors: Dora Onely Roblero-Mejía, Carlos García-Ausencio, Romina Rodríguez-Sanoja, Fernando Guzmán-Chávez, Sergio Sánchez
Format: Article
Language:English
Published: MDPI AG 2024-12-01
Series:Antibiotics
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Online Access:https://www.mdpi.com/2079-6382/13/12/1179
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Summary: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.
ISSN:2079-6382