期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 29, 页码 11763-11768出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201916321
关键词
antiviral agents; biosynthesis; ornithine; peptides; RiPPs
资金
- EU (SYNPEPTIDE)
- ETH Postdoctoral Fellowship
Proteusins are a family of bacterial ribosomal peptides that largely remain hypothetical genome-predicted metabolites. The only known members are the polytheonamide-type cytotoxins, which have complex structures due to numerous unusual posttranslational modifications (PTMs). Cyanobacteria contain large numbers of putative proteusin loci. To investigate their chemical and pharmacological potential beyond polytheonamide-type compounds, we characterized landornamide A, the product of the silent osp gene cluster from Kamptonema sp. PCC 6506. Pathway reconstruction in E. coli revealed a peptide combining lanthionines, d-residues, and, unusually, two ornithines introduced by the arginase-like enzyme OspR. Landornamide A inhibited lymphocytic choriomeningitis virus infection in mouse cells, thus making it one of the few known anti-arenaviral compounds. These data support proteusins as a rich resource of chemical scaffolds, new maturation enzymes, and bioactivities.
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