ArticleJournal of natural products2013
The presence of two cyclase thioesterases expands the conformational freedom of the cyclic Peptide occidiofungin.
Article in Journal of natural products, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Natural products shape microbial ecology and disease in the cystic fibrosis airway.Natural product reports · 2026Review
- 4-Hydroxy-3-Methyl-2-Alkenylquinoline Disrupts Temporospatial Control of Flagellar Assembly and Induces Transcriptomic Remodeling inMolecules (Basel, Switzerland) · 2026Article
- Article
- Previously Uncharacterized Variants, OCF-E-OCF-J, of the Antifungal Occidiofungin Produced byJournal of natural products · 2024Article
- Intravaginal Gel for Sustained Delivery of Occidiofungin and Long-Lasting Antifungal Effects.Gels (Basel, Switzerland) · 2023Article
- Discovery of phosphorylated lantibiotics with proimmune activity that regulate the oral microbiome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Occidiofungin: Actin Binding as a Novel Mechanism of Action in an Antifungal Agent.Antibiotics (Basel, Switzerland) · 2022Review
- Drug discovery through the isolation of natural products from Burkholderia.Expert opinion on drug discovery · 2021Review
- Formulation, Pharmacological Evaluation, and Efficacy Studies of Occidiofungin, a Novel Antifungal.Antimicrobial agents and chemotherapy · 2020Article
- Covalent Structure and Bioactivity of the Type AII Lantibiotic Salivaricin A2.Applied and environmental microbiology · 2018Article
- Comparative genome-wide analysis reveals that Burkholderia contaminans MS14 possesses multiple antimicrobial biosynthesis genes but not major genetic loci required for pathogenesis.MicrobiologyOpen · 2016Article
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Authors and funding
5 authors.
Funding
Abstract
Occidiofungin is a cyclic nonribosomally synthesized antifungal peptide with submicromolar activity produced by the Gram-negative bacterium Burkholderia contaminans. The biosynthetic gene cluster was confirmed to contain two cyclase thioesterases. NMR analysis revealed that the presence of both thioesterases is used to increase the conformational repertoire of the cyclic peptide. The loss of the OcfN cyclic thioesterase by mutagenesis results in a reduction of conformational variants and an appreciable decrease in bioactivity against Candida species. Presumably, the presence of both asparagine and β-hydroxyasparagine variants coordinates the enzymatic function of both of the cyclase thioesterases. OcfN has presumably evolved to be part of the biosynthetic gene cluster due to its ability to produce structural variants that enhance antifungal activity against some fungi. The enhancement of the antifungal activity from the incorporation of an additional cyclase thioesterase into the biosynthetic gene cluster of occidiofungin supports the need to explore new conformational variants of other therapeutic or potentially therapeutic cyclic peptides.
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