ArticlePNAS nexus2024
Subclass IId bacteriocins targeting mannose phosphotransferase system-Structural diversity and implications for receptor interaction and antimicrobial activity.
Article in PNAS nexus, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Lactic acid bacteria and their bacteriocins: promising food safety tools for controlling the foodborne pathogen Listeria monocytogenes.World journal of microbiology & biotechnology · 2026Review
- Genome-guided antimicrobial potential of Bacillus stercoris from coastal sand with activity against multidrug-resistant bacteria, including MRSA.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- Investigation of the Antibacterial Effectiveness of Hybrid Recombinant Bacteriocins Circular Enterocin and Pyocin L1 Derived from Pseudomonas aeruginosa and Enterococcus faecalis.Biochemical genetics · 2026Article
- Structural basis for the extended-spectrum antimicrobial activity of Garvieacin Q.Applied and environmental microbiology · 2026Article
- The phage shock protein response of Listeria monocytogenes influences tolerance to the multipeptide bacteriocin garvicin KS.Applied microbiology and biotechnology · 2026Article
- Solution Structure of the Broad-Spectrum Bacteriocin Garvicin Q.International journal of molecular sciences · 2025Article
- Co-Fermentation and Genomic Insights into Lactic Acid Bacteria for Enhanced Propionic Acid Production Using a Non-GMO Approach.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial mannose phosphotransferase system (Man-PTS) mediates uptake of selected monosaccharides. Simultaneously, it is a receptor for diverse bacteriocins such as subclass IIa pediocin-like bacteriocins and some subclass IId ones (garvicins ABCQ, lactococcins ABZ, BacSJ, ubericin K, and angicin). So far, no attempt has been made to categorize this ever-expanding group of bacteriocins. Here, we identified Man-PTS as a receptor for a number of previously uncharacterized bacteriocins, and demonstrated that they all belong to a large family of Man-PTS-binding nonpediocin-like peptides, providing new insights into their structure and function. Based on amino acid sequence similarities between members of this family, we propose their classification into five groups. This classification conveniently distinguishes bacteriocins with specific structures and properties regarding their spectrum of antimicrobial activity and pattern of interaction with Man-PTS. With respect to the latter, we indicate individual amino acid residues or regions of Man-PTS and the bacteriocin responsible for their interaction. In Man-PTS, these residues localize to the exterior of the transport complex, specifically the extracellular loop of the so-called Vmotif domain-containing regions
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