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The only known members are the polytheonamide\u2010type 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\u2010type compounds, we characterized landornamide\u2005A, the product of the silent\n                    <jats:italic>osp<\/jats:italic>\n                    gene cluster from\n                    <jats:italic>Kamptonema<\/jats:italic>\n                    sp. PCC 6506. Pathway reconstruction in\n                    <jats:italic>E. coli<\/jats:italic>\n                    revealed a peptide combining lanthionines,\n                    <jats:sc>d<\/jats:sc>\n                    \u2010residues, and, unusually, two ornithines introduced by the arginase\u2010like enzyme OspR. Landornamide\u2005A inhibited lymphocytic choriomeningitis virus infection in mouse cells, thus making it one of the few known anti\u2010arenaviral compounds. These data support proteusins as a rich resource of chemical scaffolds, new maturation enzymes, and bioactivities.\n                  <\/jats:p>","DOI":"10.1002\/anie.201916321","type":"journal-article","created":{"date-parts":[[2020,3,12]],"date-time":"2020-03-12T13:19:37Z","timestamp":1584019177000},"page":"11763-11768","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":73,"title":["Landornamides: Antiviral Ornithine\u2010Containing Ribosomal Peptides Discovered through Genome Mining"],"prefix":"10.1002","volume":"59","author":[{"given":"Nina M.","family":"B\u00f6sch","sequence":"first","affiliation":[{"name":"Institute of Microbiology Eidgen\u00f6ssische Technische Hochschule (ETH) Zurich  Vladimir-Prelog-Weg 4 8093 Zurich Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariana","family":"Borsa","sequence":"additional","affiliation":[{"name":"Institute of Microbiology Eidgen\u00f6ssische Technische 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