Structure of microcin B-like compounds produced by pseudomonas syringae and species specificity of their antibacterial action

Mikhail Metelev, Marina Serebryakov, Dmitry Ghilarov, Youfu Zhao, Konstantin Severinov

Research output: Contribution to journalArticlepeer-review

Abstract

Escherichia coli microcin B (Ec-McB) is a posttranslationally modified antibacterial peptide containing multiple oxazole and thiazole heterocycles and targeting the DNA gyrase. We have found operons homologous to the Ec-McB biosynthesis-immunity operon mcb in recently sequenced genomes of several pathovars of the plant pathogen Pseudomonas syringae, and we produced two variants of P. syringae microcin B (Ps-McB) in E. coli by heterologous expression. Like Ec-McB, both versions of Ps-McB target the DNA gyrase, but unlike Ec-McB, they are active against various species of the Pseudomonas genus, including human pathogen P. aeruginosa. Through analysis of Ec-McB/Ps-McB chimeras, we demonstrate that three centrally located unmodified amino acids of Ps-McB are sufficient to determine activity against Pseudomonas, likely by allowing specific recognition by a transport system that remains to be identified. The results open the way for construction of McB-based antibacterial molecules with extended spectra of biological activity.

Original languageEnglish (US)
Pages (from-to)4129-4137
Number of pages9
JournalJournal of bacteriology
Volume195
Issue number18
DOIs
StatePublished - 2013

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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