ArticleHuman molecular genetics2015
Anti-Aβ single-chain variable fragment antibodies exert synergistic neuroprotective activities in Drosophila models of Alzheimer's disease.
Article in Human molecular genetics, 2015. 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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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
11 citing papers in PubMed, 19 citations in OpenAlex.
- A C1qTNF3 collagen domain fusion chaperones diverse secreted proteins and anti-Aβ scFvs: Applications for gene therapies.Molecular therapy. Methods & clinical development · 2023Article
- A monocarboxylate transporter rescues frontotemporal dementia and Alzheimer's disease models.PLoS genetics · 2023Article
- Application of Antibody Fragments Against Aβ With Emphasis on Combined Application With Nanoparticles in Alzheimer's Disease.Frontiers in pharmacology · 2021Review
- Intramuscular injection of vectorized-scFvMC1 reduces pathological tau in two different tau transgenic models.Acta neuropathologica communications · 2020Article
- Neuronally expressed anti-tau scFv prevents tauopathy-induced phenotypes in Drosophila models.Neurobiology of disease · 2020Review
- Pharmacokinetic parameters and mechanism of action of an efficient anti-Aβ single chain antibody fragment.PloS one · 2019Article
- Anti-Aβ single-chain variable fragment antibodies restore memory acquisition in a Drosophila model of Alzheimer's disease.Scientific reports · 2017Article
- Combined effects of scanning ultrasound and a tau-specific single chain antibody in a tau transgenic mouse model.Brain : a journal of neurology · 2017Article
- Phenotypic differences betweenAnimal cells and systems · 2017Article
- Holdase activity of secreted Hsp70 masks amyloid-β42 neurotoxicity in Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Both active and passive immunotherapy protocols decrease insoluble amyloid-ß42 (Aß42) peptide in animal models, suggesting potential therapeutic applications against the main pathological trigger in Alzheimer's disease (AD). However, recent clinical trials have reported no significant benefits from humanized anti-Aß42 antibodies. Engineered single-chain variable fragment antibodies (scFv) are much smaller and can easily penetrate the brain, but identifying the most effective scFvs in murine AD models is slow and costly. We show here that scFvs against the N- and C-terminus of Aß42 (scFv9 and scFV42.2, respectively) that decrease insoluble Aß42 in CRND mice are neuroprotective in Drosophila models of Aß42 and amyloid precursor protein neurotoxicity. Both scFv9 and scFv42.2 suppress eye toxicity, reduce cell death in brain neurons, protect the structural integrity of dendritic terminals in brain neurons and delay locomotor dysfunction. Additionally, we show for the first time that co-expression of both anti-Aß scFvs display synergistic neuroprotective activities, suggesting that combined therapies targeting distinct Aß42 epitopes can be more effective than targeting a single epitope. Overall, we demonstrate the feasibility of using Drosophila as a first step for characterizing neuroprotective anti-Aß scFvs in vivo and identifying scFv combinations with synergistic neuroprotective activities.
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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.