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Landornamides: Antiviral Ornithine-Containing Ribosomal Peptides Discovered through Genome Mining

Abstract : Proteusins are a family of bacterial ribosomal peptides that largely remain hypothetical genome-predicted metabolites. The only known members are the polytheona-mide-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 lym-phocytic 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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Submitted on : Wednesday, May 27, 2020 - 3:07:52 PM
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Nina Bösch, Mariana Borsa, Ute Greczmiel, Brandon I Morinaka, Muriel Gugger, et al.. Landornamides: Antiviral Ornithine-Containing Ribosomal Peptides Discovered through Genome Mining. Angewandte Chemie International Edition, 2020, ⟨10.1002/anie.201916321⟩. ⟨pasteur-02634375⟩



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