ArticleBMC microbiology2021
Proteomic response of Escherichia coli to a membrane lytic and iron chelating truncated Amaranthus tricolor defensin.
Article in BMC microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Antimicrobial Potential of Defensin-DerivedInternational journal of molecular sciences · 2026Article
- TheJournal of proteome research · 2026Article
- Proteomic Analysis Revealed that DVL, a Lectin Purified fromACS omega · 2025Article
- Identification and Characterization of CC-AMP1-like and CC-AMP2-like Peptides inJournal of proteome research · 2024Article
- Transcriptome-Wide Identification and Expression Analysis of Genes Encoding Defense-Related Peptides ofJournal of fungi (Basel, Switzerland) · 2024Article
- The Greater Celandine: Identification and Characterization of an Antimicrobial Peptide fromJournal of natural products · 2024Article
- No Chance to Survive:Antibiotics (Basel, Switzerland) · 2023Article
- The γ-Core Motif Peptides of Plant AMPs as Novel Antimicrobials for Medicine and Agriculture.International journal of molecular sciences · 2022Review
- New Insights into the Mechanism of Antibacterial Action of Synthetic PeptideAntibiotics (Basel, Switzerland) · 2022Article
- Creating optimized peptide libraries for AMP discovery via PepSAVI-MS.Methods in enzymology · 2022Article
- Mass Spectrometric Identification of Antimicrobial Peptides from Medicinal Seeds.Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundPlant defensins are a broadly distributed family of antimicrobial peptides which have been primarily studied for agriculturally relevant antifungal activity. Recent studies have probed defensins against Gram-negative bacteria revealing evidence for multiple mechanisms of action including membrane lysis and ribosomal inhibition. Herein, a truncated synthetic analog containing the γ-core motif of Amaranthus tricolor DEF2 (Atr-DEF2) reveals Gram-negative antibacterial activity and its mechanism of action is probed via proteomics, outer membrane permeability studies, and iron reduction/chelation assays.
resultsAtr-DEF2(G39-C54) demonstrated activity against two Gram-negative human bacterial pathogens, Escherichia coli and Klebsiella pneumoniae. Quantitative proteomics revealed changes in the E. coli proteome in response to treatment of sub-lethal concentrations of the truncated defensin, including bacterial outer membrane (OM) and iron acquisition/processing related proteins. Modification of OM charge is a common response of Gram-negative bacteria to membrane lytic antimicrobial peptides (AMPs) to reduce electrostatic interactions, and this mechanism of action was confirmed for Atr-DEF2(G39-C54) via an N-phenylnaphthalen-1-amine uptake assay. Additionally, in vitro assays confirmed the capacity of Atr-DEF2(G39-C54) to reduce Fe
conclusionsThis study highlights the utility of plant defensin γ-core motif synthetic analogs for characterization of novel defensin activity. Proteomic changes in E. coli after treatment with Atr-DEF2(G39-C54) supported the hypothesis that membrane lysis is an important component of γ-core motif mediated antibacterial activity but also emphasized that other properties, such as metal sequestration, may contribute to a multifaceted mechanism of action.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.