Heterologous expression and functional characterization of novel microcin B17 congeners from environmental Pseudomonas isolates

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Authors: Sandrien De Smedt, Dries Wéry, Hanne Vande Capelle, Hans Gerstmans, Pieter Monsieurs, Joleen Masschelein, Philip Ruelens, Maarten Fauvart, Jan Michiels
Cited by: 1
References: 45

Abstract

Microcin B17 (MccB17) is a ribosomally synthesized and post-translationally modified peptide (RiPP) with antibacterial activity, natively produced by Escherichia coli. Despite its unique gyrase-inhibiting activity, therapeutic development has been limited, primarily due to its low solubility and narrow spectrum of activity. Here, we employed a genome mining approach to identify and functionally characterize novel MccB17-like biosynthetic gene clusters (BGCs) from uncharacterized environmental Pseudomonas isolates. Four BGCs sharing substantial sequence similarity were cloned and heterologously expressed in E. coli. Regardless of their similarity, the clusters triggered congener-dependent growth retardation and cell elongation, despite lacking detectable antibacterial activity in overlay assays. Transcription and production of modified MccB17-like peptides or their unmodified precursors were confirmed by reverse transcription-quantitative PCR (RT-qPCR) and liquid chromatography-mass spectrometry (LC-MS), respectively. Transcriptome profiling indicated differential induction of stress responses and metabolic shifts in host cells, with limited overlap among the different BGCs. Our findings suggest that structurally similar MccB17 congeners can elicit distinct physiological responses. This study expands the known range of MccB17-like RiPPs and highlights the importance of functionally exploring RiPP diversity beyond known antimicrobial activity, even among congeners. KEY POINTS: • In silico identification of uncharacterized MccB17 congeners from Pseudomonas spp. • Functional analysis of novel variants reveals phenotypic effects on expression host • Transcriptomics reveals congener-specific effects despite similarity to E. coli MccB17.

Fields of Study & Subjects

Microbial Natural Products and Biosynthesis Antimicrobial Peptides and Activities Peptidase Inhibition and Analysis

Publication details

Journal / source
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Volume
110
Issue
1
Pages
45–45
Publication date
29 January 2026
Language
EN