ArticleScientific reports2017
Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Studying the mechanisms of neurodegeneration:Frontiers in cellular neuroscience · 2025Review
- Rescue of ApoE4-related lysosomal autophagic failure in Alzheimer's disease by targeted small molecules.Communications biology · 2024Article
- Redox-Responsive Polymeric Nanogels as Efficient mRNA Delivery Vehicles inmicroPublication biology · 2024Article
- Unraveling effects of anti-aging drugs on C. elegans using liposomes.GeroScience · 2023Article
- Review
- A Combined Cell-Worm Approach to Search for Compounds Counteracting the Toxicity of Tau Oligomers In Vivo.International journal of molecular sciences · 2022Article
- Extracellular Vesicles From Microalgae: Uptake Studies in Human Cells andFrontiers in bioengineering and biotechnology · 2022Article
- Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans.Scientific reports · 2021Article
- Comparative Studies in the A30P and A53T α-SynucleinFrontiers in cell and developmental biology · 2021Article
- A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.Scientific reports · 2020Article
- Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture.Nature chemistry · 2020Article
- Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification.ACS central science · 2019Article
- Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies.ACS chemical biology · 2019Article
- α-Sheet secondary structure in amyloid β-peptide drives aggregation and toxicity in Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nematode worm Caenorhabditis elegans (C. elegans) is a versatile and widely used animal model for in vivo studies of a broad range of human diseases, in particular for understanding their genetic origins and for screening drug candidates. Nevertheless, the challenges associated with the administration of native proteins to C. elegans have limited the range of applications of this animal model in protein-based drug discovery programs. Here, we describe a readily usable protocol for the transduction of native proteins in C. elegans, which is based on the encapsulation of the proteins of interest within cationic lipid vesicles, prior to their administration to worms. This procedure limits the degradation of the proteins in the guts of the animals, and promotes their adsorption into body tissues. To illustrate the efficacy of this approach we apply it to deliver an antibody designed to inhibit α-synuclein aggregation, and show that it can lead to the rescue of the disease phenotype in a C. elegans model of Parkinson's disease. As this transduction protocol is fast and inexpensive, we anticipate that it will be readily applicable to protein-based drug discovery studies that utilize C. elegans as a model organism.
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