Highly efficient intercellular spreading of protein misfolding mediated by viral ligand-receptor interactions

Autor: Shu Liu, André Hossinger, Stefanie-Elisabeth Heumüller, Annika Hornberger, Oleksandra Buravlova, Katerina Konstantoulea, Stephan A. Müller, Lydia Paulsen, Frederic Rousseau, Joost Schymkowitz, Stefan F. Lichtenthaler, Manuela Neumann, Philip Denner, Ina M. Vorberg

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)

Pathologic protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells via extracellular vesicles or direct cell-to-cell contact. Here, Liu et al. show that viral glycoproteins can contribute to inte

Externí odkaz: https://doaj.org/article/3c987601848e42e7821270559f3b20a9

Prion strains depend on different endocytic routes for productive infection

Autor: Andrea Fehlinger, Hanna Wolf, André Hossinger, Yvonne Duernberger, Catharina Pleschka, Katrin Riemschoss, Shu Liu, Romina Bester, Lydia Paulsen, Suzette A. Priola, Martin H. Groschup, Hermann M. Schätzl, Ina M. Vorberg

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)

Abstract Prions are unconventional agents composed of misfolded prion protein that cause fatal neurodegenerative diseases in mammals. Prion strains induce specific neuropathological changes in selected brain areas. The mechanism of strain-specific ce

Externí odkaz: https://doaj.org/article/13fe002f36ce4b6588374aa799d3ba3e

Endogenous retroviruses promote prion-like spreading of proteopathic seeds

Autor: Shu Liu, Stefanie-Elisabeth Heumüller, André Hossinger, Stephan A. Müller, Oleksandra Buravlova, Stefan F. Lichtenthaler, Philip Denner, Ina M. Vorberg

Endogenous retroviruses, remnants of viral germline infections, make up a substantial proportion of the mammalian genome. While usually epigenetically silenced, retroelements can become upregulated in neurodegenerative diseases associated with protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1f3c2ebb90a8b8c91f07a003919a604c
https://doi.org/10.1101/2022.05.06.490866

Highly efficient intercellular spreading of protein misfolding mediated by viral ligand - receptor interactions

Autor: Manuela Neumann, André Hossinger, Stefan F. Lichtenthaler, Philip Denner, Annika Hornberger, Ina Vorberg, Shu Liu, Oleksandra Buravlova, Stephan A. Müller

SUMMARYPathological protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells, thereby templating their own aberrant conformation onto soluble proteins of the same kind. Proteopathic seeds can be r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1e9e1c87efcb9c00bfa539cb49e8d91b
https://doi.org/10.1101/2020.06.26.173070

Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells

Autor: Shu Liu, Yvonne Duernberger, Katrin Riemschoss, Benedetta Bolognesi, Annika Hornberger, Oleksandra Buravlova, Stephan A. Müller, Lydia Paulsen, Ina Vorberg, Philipp von Eisenhart-Rothe, Stefan F. Lichtenthaler, André Hossinger, Gian Gaetano Tartaglia, Verena Arndt, Sebastian Hogl, Nieves Lorenzo-Gotor

Publikováno v: Life Science Alliance
Recercat. Dipósit de la Recerca de Catalunya
instname
Life science alliance 2(4), e201800280 (2019). doi:10.26508/lsa.201800280

This study provides evidence that exogenous proteinaceous seeds can induce protein aggregates that sequester stress granule components independent of stress granule assembly.
Prions of lower eukaryotes are self-templating protein aggregates that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::519833838ae0f8065a48060f79452133
http://hdl.handle.net/10230/42509