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Publication Abstract from PubMed

We report the heterologous expression, structure, and antimicrobial activity of a lasso peptide, ubonodin, encoded in the genome of Burkholderia ubonensis . The topology of ubonodin is unprecedented amongst lasso peptides with 18 of its 28 amino acids found in the mechanically-bonded loop segment. Ubonodin inhibits RNA polymerase in vitro and has potent antimicrobial activity against several pathogenic members of the Burkholderia genus, most notably B. cepacia and B. multivorans , causative agents of lung infections in cystic fibrosis patients.

Discovery of ubonodin, an antimicrobial lasso peptide active against members of the Burkholderia cepacia complex.,Cheung-Lee WL, Parry M, Zong C, Jaramillo Cartagena A, Darst S, Connell N, Russo R, Link AJ Chembiochem. 2019 Nov 25. doi: 10.1002/cbic.201900707. PMID:31765515^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.