| Literature DB >> 31765515 |
Wai Ling Cheung-Lee1, Madison E Parry1, Chuhan Zong2, Alexis Jaramillo Cartagena3, Seth A Darst3, Nancy D Connell4, Riccardo Russo5, A James Link1,2,6.
Abstract
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.Entities:
Keywords: RiPP; antibiotics; lasso peptides; natural products; peptides
Year: 2020 PMID: 31765515 PMCID: PMC7205569 DOI: 10.1002/cbic.201900707
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164