{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(1)"],"submitter":["Liu S"],"pubmed_abstract":["Protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells, thereby templating their own aberrant conformation onto soluble homotypic proteins. Proteopathic seeds can be released into the extracellular space, secreted in association with extracellular vesicles (EV) or exchanged by direct cell-to-cell contact. The extent to which each of these pathways contribute to the prion-like spreading of protein misfolding is unclear. Exchange of cellular cargo by both direct cell contact or via EV depends on receptor-ligand interactions. We hypothesized that enabling these interactions through viral ligands enhances intercellular proteopathic seed transmission. Using different cellular models propagating prions or pathogenic Tau aggregates, we demon"],"journal":["Nature communications"],"pagination":["5739"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8526834"],"repository":["biostudies-literature"],"pubmed_title":["Highly efficient intercellular spreading of protein misfolding mediated by viral ligand-receptor interactions."],"pmcid":["PMC8526834"],"pubmed_authors":["Hornberger A","Buravlova O","Schymkowitz J","Vorberg IM","Hossinger A","Rousseau F","Denner P","Liu S","Neumann M","Lichtenthaler SF","Muller SA","Heumuller SE","Konstantoulea K","Paulsen L"],"additional_accession":[]},"is_claimable":false,"name":"Highly efficient intercellular spreading of protein misfolding mediated by viral ligand-receptor interactions.","description":"Protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells, thereby templating their own aberrant conformation onto soluble homotypic proteins. Proteopathic seeds can be released into the extracellular space, secreted in association with extracellular vesicles (EV) or exchanged by direct cell-to-cell contact. The extent to which each of these pathways contribute to the prion-like spreading of protein misfolding is unclear. Exchange of cellular cargo by both direct cell contact or via EV depends on receptor-ligand interactions. We hypothesized that enabling these interactions through viral ligands enhances intercellular proteopathic seed transmission. Using different cellular models propagating prions or pathogenic Tau aggregates, we demon","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2025-04-18T17:28:03.104Z","creation":"2025-02-19T00:19:02.624Z"},"accession":"S-EPMC8526834","cross_references":{"pubmed":["34667166"],"doi":["10.1038/s41467-021-25855-2"]}}