Discovery of Ubonodin, an Antimicrobial Lasso Peptide Active against Members of the Burkholderia cepacia Complex
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. U...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2020-05, Vol.21 (9), p.1335-1340 |
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| container_title | Chembiochem : a European journal of chemical biology |
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| creator | Cheung‐Lee, Wai Ling Parry, Madison E. Zong, Chuhan Cartagena, Alexis Jaramillo Darst, Seth A. Connell, Nancy D. Russo, Riccardo Link, A. James |
| description | 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.
Roping in lung infections: Ubonodin is a novel lasso peptide discovered by genome mining in a strain of Burkholderia. It has an unprecedented topology for a lasso peptide with an 18 aa mechanically bonded loop. Ubonodin exhibits potent antimicrobial activity against pathogenic Burkholderia species. |
| doi_str_mv | 10.1002/cbic.201900707 |
| format | Article |
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Roping in lung infections: Ubonodin is a novel lasso peptide discovered by genome mining in a strain of Burkholderia. It has an unprecedented topology for a lasso peptide with an 18 aa mechanically bonded loop. Ubonodin exhibits potent antimicrobial activity against pathogenic Burkholderia species.</description><subject>Amino acids</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>antibiotics</subject><subject>Antiinfectives and antibacterials</subject><subject>Antimicrobial activity</subject><subject>Antimicrobial agents</subject><subject>Bronchopulmonary infection</subject><subject>Burkholderia</subject><subject>Burkholderia cepacia complex - classification</subject><subject>Burkholderia cepacia complex - drug effects</subject><subject>Cystic fibrosis</subject><subject>DNA-directed RNA polymerase</subject><subject>DNA-Directed RNA Polymerases - antagonists & inhibitors</subject><subject>Drug Discovery</subject><subject>Genomes</subject><subject>Humans</subject><subject>lasso peptides</subject><subject>natural products</subject><subject>Peptides</subject><subject>Pore Forming Cytotoxic Proteins - chemistry</subject><subject>Pore Forming Cytotoxic Proteins - pharmacology</subject><subject>RiPP</subject><subject>RNA polymerase</subject><subject>Topology</subject><issn>1439-4227</issn><issn>1439-7633</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuP0zAURi0EYobCliWyxIYFLXYcx_EGqRNeIxXBgllbftxMPSRxsJNC_z2uWspjw8qW7vGR7_ch9JSSFSWkeGWNt6uCUEmIIOIeuqQlk0tRMXb_dC-LQlygRyndEUJkxehDdMGoqDin_BKNb3yyYQdxj0OLb0wYgvPDS6wHvB4m33sbg_G6wxudUsCfYZy8A7y2k98B1rfaD2nCH6E3ENNBMW0BX83x6zZ0DqLX2MKobT6b0I8d_HiMHrS6S_DkdC7Qzbu3X5oPy82n99fNerO0XFCxrHRduKK0xhDZstpZw620wEXpyrqljNWiJpWR3ORZWxOujROWWM64M6WxbIFeH73jbHpwFoYp6k6N0fc67lXQXv09GfxW3YadEgXhvJJZ8OIkiOHbDGlSfY4Kuk4PEOakCkZrwZjMIS_Q83_QuzDHIa-XKVmXLEdNMrU6UjnSlCK0589Qog5lqkOZ6lxmfvDszxXO-K_2MiCPwHffwf4_OtVcXTe_5T8BLtWtVw</recordid><startdate>20200504</startdate><enddate>20200504</enddate><creator>Cheung‐Lee, Wai Ling</creator><creator>Parry, Madison E.</creator><creator>Zong, Chuhan</creator><creator>Cartagena, Alexis Jaramillo</creator><creator>Darst, Seth A.</creator><creator>Connell, Nancy D.</creator><creator>Russo, Riccardo</creator><creator>Link, A. 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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.
Roping in lung infections: Ubonodin is a novel lasso peptide discovered by genome mining in a strain of Burkholderia. It has an unprecedented topology for a lasso peptide with an 18 aa mechanically bonded loop. Ubonodin exhibits potent antimicrobial activity against pathogenic Burkholderia species.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>31765515</pmid><doi>10.1002/cbic.201900707</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-5066-9691</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antibiotics Antiinfectives and antibacterials Antimicrobial activity Antimicrobial agents Bronchopulmonary infection Burkholderia Burkholderia cepacia complex - classification Burkholderia cepacia complex - drug effects Cystic fibrosis DNA-directed RNA polymerase DNA-Directed RNA Polymerases - antagonists & inhibitors Drug Discovery Genomes Humans lasso peptides natural products Peptides Pore Forming Cytotoxic Proteins - chemistry Pore Forming Cytotoxic Proteins - pharmacology RiPP RNA polymerase Topology |
| title | Discovery of Ubonodin, an Antimicrobial Lasso Peptide Active against Members of the Burkholderia cepacia Complex |
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