ArticleJournal of the American Chemical Society2014
Molecular basis for self-assembly of a human host-defense peptide that entraps bacterial pathogens.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 94 citations in OpenAlex.
- Article
- Serine protease HtrA promotesScience advances · 2026Article
- Dual-functional self-assembled nanosystems with enhanced protease resistance: Promoting bacterial aggregation and immune activation for multidrug-resistant bacterial infection.Asian journal of pharmaceutical sciences · 2026Article
- Article
- Fighting the invader: strategies against intracellular bacteria.Frontiers in pharmacology · 2026Review
- Calprotectin-mediated survival ofmBio · 2025Article
- Intestinal biofilms: pathophysiological relevance, host defense, and therapeutic opportunities.Clinical microbiology reviews · 2024Review
- "Live" Nanomaterials Process Biomimetic Recognition and Assembly In Vivo.Small science · 2023Article
- Amyloid-like nanofibrous network confined and aligned ultrafine bimetallic nanozymes for smart antibacterial therapy.Materials today. Bio · 2023Article
- AIEgen-Based Nanomaterials for Bacterial Imaging and Antimicrobial Applications: Recent Advances and Perspectives.Molecules (Basel, Switzerland) · 2023Review
- Flagella-driven motility is a target of human Paneth cell defensin activity.PLoS pathogens · 2023Article
- Antimicrobial peptides´ immune modulation role in intracellular bacterial infection.Frontiers in immunology · 2023Review
- Human α-Defensin-6 NeutralizesInternational journal of molecular sciences · 2022Article
- Evolving and assembling to pierce through: Evolutionary and structural aspects of antimicrobial peptides.Computational and structural biotechnology journal · 2022Review
- Flagella at the Host-Microbe Interface: Key Functions Intersect With Redundant Responses.Frontiers in immunology · 2022Review
- Recent Advances and Challenges in Nanodelivery Systems for Antimicrobial Peptides (AMPs).Antibiotics (Basel, Switzerland) · 2021Review
- De novo design of a pH-triggered self-assembled β-hairpin nanopeptide with the dual biological functions for antibacterial and entrapment.Journal of nanobiotechnology · 2021Article
- Article
- Pathogen-specific antimicrobials engineered de novo through membrane-protein biomimicry.Nature biomedical engineering · 2021Article
- Nanostructured Antimicrobial Peptides: Crucial Steps of Overcoming the Bottleneck for Clinics.Frontiers in microbiology · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Human α-defensin 6 (HD6) is a 32-aa cysteine-rich peptide of the innate immune system. Although HD6 is a member of an antimicrobial peptide family, it exhibits negligible antibacterial activity in vitro. Rather, HD6 possesses a unique innate immune mechanism whereby it self-assembles into oligomers that capture pathogens to prevent microbial invasion of the intestinal epithelium and subsequent dissemination. Molecular-level understanding for why HD6 functions differently from other human defensins remains unclear. To further elucidate the HD6 self-assembly process and its biological activity, we developed robust protocols for obtaining native and mutant HD6 in high purity from overexpression in Escherichia coli. We combined biophysical characterization with biological assays to probe HD6 structure and function. We report that native HD6 readily self-assembles into elongated fibrils observable by transmission electron microscopy, agglutinates both Gram-negative and -positive bacteria, and prevents the human gastrointestinal pathogen Listeria monocytogenes from invading cultured mammalian cells. Mutation of hydrophobic residues (F2A, I22T, V25T, F29A) perturbs self-assembly and results in attenuated biological activity. In particular, the F2A and F29A mutants do not form fibrils under our experimental conditions and neither agglutinate bacteria nor prevent L. monocytogenes invasion. In total, our results demonstrate that the hydrophobic effect is essential for promoting HD6 self-assembly and innate immune function, and indicate that HD6 may provide host defense against Listeria in the gut. This investigation provides a timely description of how variations in amino acid sequence confer diverse physiological functions to members of the defensin family.
Indexed as
Identifiers
What OpenQuestion holds
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.