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Discovery, Characterization, and Bioactivity of the Achromonodins: Lasso Peptides Encoded by Achromobacter.
Carson, Drew V; Zhang, Yi; So, Larry; Cheung-Lee, Wai Ling; Cartagena, Alexis Jaramillo; Darst, Seth A; Link, A James.
Afiliación
  • Carson DV; Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.
  • Zhang Y; Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.
  • So L; Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.
  • Cheung-Lee WL; Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.
  • Cartagena AJ; Laboratory of Molecular Biophysics and Tri-Institutional Training Program in Chemical Biology, Rockefeller University, New York, New York 10065, United States.
  • Darst SA; Laboratory of Molecular Biophysics and Tri-Institutional Training Program in Chemical Biology, Rockefeller University, New York, New York 10065, United States.
  • Link AJ; Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.
J Nat Prod ; 86(11): 2448-2456, 2023 11 24.
Article en En | MEDLINE | ID: mdl-37870195
Through genome mining efforts, two lasso peptide biosynthetic gene clusters (BGCs) within two different species of Achromobacter, a genus that contains pathogenic organisms that can infect patients with cystic fibrosis, were discovered. Using gene-refactored BGCs in E. coli, these lasso peptides, which were named achromonodin-1 and achromonodin-2, were heterologously expressed. Achromonodin-1 is naturally encoded by certain isolates from the sputum of patients with cystic fibrosis. The NMR structure of achromonodin-1 was determined, demonstrating that it is a threaded lasso peptide with a large loop and short tail structure, reminiscent of previously characterized lasso peptides that inhibit RNA polymerase (RNAP). Achromonodin-1 inhibits RNAP in vitro and has potent, focused activity toward Achromobacter pulmonis, another isolate from the sputum of a cystic fibrosis patient. These efforts expand the repertoire of antimicrobial lasso peptides and provide insights into how Achromobacter isolates from certain ecological niches interact with each other.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fibrosis Quística / Achromobacter Límite: Humans Idioma: En Revista: J Nat Prod Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fibrosis Quística / Achromobacter Límite: Humans Idioma: En Revista: J Nat Prod Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos