ArticleBiochemistry2015
Visualizing attack of Escherichia coli by the antimicrobial peptide human defensin 5.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 101 citations in OpenAlex.
- Antimicrobial peptides: structure, functions and translational applications.Nature reviews. Microbiology · 2025Review
- Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes.Biomolecules · 2025Article
- Explainable deep learning and virtual evolution identifies antimicrobial peptides with activity against multidrug-resistant human pathogens.Nature microbiology · 2025Article
- STAT1/MUC4 activation promotes antimicrobial peptide production to reduce intestinal epithelium barrier injury caused by enteropathogenicArchives of medical science : AMS · 2025Article
- Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides.PloS one · 2025Article
- Review
- The Antimicrobial Activity of Human Defensins at Physiological Non-Permeabilizing Concentrations Is Caused by the Inhibition of the Plasma Membrane HInternational journal of molecular sciences · 2024Article
- Peptide Dendrimer-Based Antibacterial Agents: Synthesis and Applications.ACS infectious diseases · 2024Review
- Protective effect and mechanism of nanoantimicrobial peptide ND-C14 againstWorld journal of emergency medicine · 2024Article
- Significance of host antimicrobial peptides in the pathogenesis and treatment of acne vulgaris.Frontiers in immunology · 2024Review
- Structural and functional insights of sortases and their interactions with antivirulence compounds.Current research in structural biology · 2024Review
- Using metabolomics to understand stress responses in Lactic Acid Bacteria and their applications in the food industry.Metabolomics : Official journal of the Metabolomic Society · 2023Review
- Ubiquitous Colonic Ileal Metaplasia Consistent with the Diagnosis of Crohn's Colitis among Indeterminate Colitis Cohorts.Medical research archives · 2023Article
- Antimicrobial Peptides in Infectious Diseases and Beyond-A Narrative Review.Life (Basel, Switzerland) · 2023Review
- Lipidation of Naturally Occurring α-Helical Antimicrobial Peptides as a Promising Strategy for Drug Design.International journal of molecular sciences · 2023Article
- Flagella-driven motility is a target of human Paneth cell defensin activity.PLoS pathogens · 2023Article
- Molecular dynamics simulations of human α-defensin 5 (HD5) crossing gram-negative bacterial membrane.PloS one · 2023Article
- Mammals' humoral immune proteins and peptides targeting the bacterial envelope: from natural protection to therapeutic applications against multidrug-resistant Gram-negatives.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Human defensin-inspired discovery of peptidomimetic antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multitalented Synthetic Antimicrobial Peptides and Their Antibacterial, Antifungal and Antiviral Mechanisms.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Human α-defensin 5 (HD5) is a 32-residue cysteine-rich host-defense peptide that exhibits broad-spectrum antimicrobial activity and contributes to innate immunity in the human gut and other organ systems. Despite many years of investigation, its antimicrobial mechanism of action remains unclear. In this work, we report that HD5ox, the oxidized form of this peptide that exhibits three regiospecific disulfide bonds, causes distinct morphological changes to Escherichia coli and other Gram-negative microbes. These morphologies include bleb formation, cellular elongation, and clumping. The blebs are up to ∼1 μm wide and typically form at the site of cell division or cell poles. Studies with E. coli expressing cytoplasmic GFP reveal that HD5ox treatment causes GFP emission to localize in the bleb. To probe the cellular uptake of HD5ox and subsequent localization, we describe the design and characterization of a fluorophore-HD5 conjugate family. By employing these peptides, we demonstrate that fluorophore-HD5ox conjugates harboring the rhodamine and coumarin fluorophores enter the E. coli cytoplasm. On the basis of the fluorescence profiles, each of these fluorophore-HD5ox conjugates localizes to the site of cell division and cell poles. These studies support the notion that HD5ox, at least in part, exerts its antibacterial activity against E. coli and other Gram-negative microbes in the cytoplasm.
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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.