ArticleScientific reports2016
Amyloidogenic amyloid-β-peptide variants induce microbial agglutination and exert antimicrobial activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
What it found
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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.
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Who cites it
74 citing papers in PubMed, 122 citations in OpenAlex.
- Pathological or preventative? Amyloid-β as an effector of innate immunity.Infection and immunity · 2026Review
- Bidirectional relationship between the biofilm ofMicrobiology spectrum · 2026Article
- Creation of New Antimicrobial Peptides 3: Research Promises and Shortcomings.International journal of molecular sciences · 2025Article
- Modulation of Amyloid-β Aggregation by Surface Proteins from Pathogens Associated with Alzheimer's Disease.ACS chemical neuroscience · 2025Article
- CD47-amyloid-β-CD74 signaling triggers adaptive immunosuppression in sepsis.EMBO reports · 2025Article
- Intraneuronal binding of amyloid beta with reelin-Implications for the onset of Alzheimer's disease.PLoS computational biology · 2025Article
- No evidence of Alzheimer's disease pathology in mice infected with Toxocara canis.Parasite (Paris, France) · 2025Article
- Review
- Do microbes play a role in Alzheimer's disease?Microbial biotechnology · 2024Article
- Lung endothelium, tau, and amyloids in health and disease.Physiological reviews · 2024Review
- Viral Infections, Are They a Trigger and Risk Factor of Alzheimer's Disease?Pathogens (Basel, Switzerland) · 2024Review
- Alzheimer's disease and infectious agents: a comprehensive review of pathogenic mechanisms and microRNA roles.Frontiers in neuroscience · 2024Review
- The oral-brain axis: can periodontal pathogens trigger the onset and progression of Alzheimer's disease?Frontiers in microbiology · 2024Review
- Neuroinflammation in Alzheimer's Disease: A Potential Role of Nose-Picking in Pathogen Entry via the Olfactory System?Biomolecules · 2023Review
- The elusive role of herpesviruses in Alzheimer's disease: current evidence and future directions.NeuroImmune pharmacology and therapeutics · 2023Review
- γ-Secretase fanning the fire of innate immunity.Biochemical Society transactions · 2023Review
- Amyloid β-based therapy for Alzheimer's disease: challenges, successes and future.Signal transduction and targeted therapy · 2023Review
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- Zn(II) binding to pramlintide results in a structural kink, fibril formation and antifungal activity.Scientific reports · 2022Article
- Human antimicrobial peptide LL-37 contributes to Alzheimer's disease progression.Molecular psychiatry · 2022Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid-β (Aβ) peptides are the main components of the plaques found in the brains of patients with Alzheimer's disease. However, Aβ peptides are also detectable in secretory compartments and peripheral blood contains a complex mixture of more than 40 different modified and/or N- and C-terminally truncated Aβ peptides. Recently, anti-infective properties of Aβ peptides have been reported. Here, we investigated the interaction of Aβ peptides of different lengths with various bacterial strains and the yeast Candida albicans. The amyloidogenic peptides Aβ1-42, Aβ2-42, and Aβ3p-42 but not the non-amyloidogenic peptides Aβ1-40 and Aβ2-40 bound to microbial surfaces. As observed by immunocytochemistry, scanning electron microscopy and Gram staining, treatment of several bacterial strains and Candida albicans with Aβ peptide variants ending at position 42 (Aβx-42) caused the formation of large agglutinates. These aggregates were not detected after incubation with Aβx-40. Furthermore, Aβx-42 exerted an antimicrobial activity on all tested pathogens, killing up to 80% of microorganisms within 6 h. Aβ1-40 only had a moderate antimicrobial activity against C. albicans. Agglutination of Aβ1-42 was accelerated in the presence of microorganisms. These data demonstrate that the amyloidogenic Aβx-42 variants have antimicrobial activity and may therefore act as antimicrobial peptides in the immune system.
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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.