1. Isolation and structure determination of a new antibacterial lanthipeptide derived from the marine derived bacterium Lysinibacillus sp.CTST325.
- Author
-
Thetsana C, Moriuchi R, and Kodani S
- Subjects
- Genome, Bacterial, Bacillaceae genetics, Bacillaceae chemistry, Bacillaceae metabolism, Peptides pharmacology, Peptides chemistry, Peptides genetics, Peptides isolation & purification, Peptides metabolism, Microbial Sensitivity Tests, Gram-Positive Bacteria drug effects, Phylogeny, Magnetic Resonance Spectroscopy, Anti-Bacterial Agents pharmacology, Anti-Bacterial Agents chemistry, Anti-Bacterial Agents isolation & purification, Multigene Family, Geologic Sediments microbiology
- Abstract
Marine resources are attractive for screening new useful bacteria. From a marine sediment sample, we performed isolation and screening of bacterial strains in search of new bioactive compounds. HPLC and ESI-MS analysis indicated that the new bacterium, Lysinibacillus sp. CTST325 (NBRC 116944), produced a new peptidic compound, lysinibacin. Genome sequence analysis of Lysinibacillus sp. CTST325 indicated the presence of several biosynthetic gene clusters for secondary metabolites, including lanthipeptides. The structure determination of lysinibacin was performed using CID-MS and NMR spectral data. As a result, lysinibacin was identified as a new class III lanthipeptide, containing N-dimethylated Tyr at the N-terminus and the unusual amino acid labionin at the C-terminus. The biosynthetic gene cluster of lysinibacin was identified from the genome data of the strain CTST325, based on the structure of lysinibacin. Lysinibacin showed antibacterial activity against Gram-positive bacteria., Competing Interests: Declarations. Competing interests: The authors declare no competing interests. Ethical approval: This study does not contain any experiments with human participants or animals., (© 2024. The Author(s), under exclusive licence to Springer Nature B.V.)
- Published
- 2025
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