Home > Publications Database > Reactivated endogenous retroviruses promote protein aggregate spreading. > print

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005     20240112171408.0
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100 1 _ |a Liu, Shu
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245 _ _ |a Reactivated endogenous retroviruses promote protein aggregate spreading.
260 _ _ |a [London]
|c 2023
|b Nature Publishing Group UK
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520 _ _ |a Prion-like spreading of protein misfolding is a characteristic of neurodegenerative diseases, but the exact mechanisms of intercellular protein aggregate dissemination remain unresolved. Evidence accumulates that endogenous retroviruses, remnants of viral germline infections that are normally epigenetically silenced, become upregulated in neurodegenerative diseases such as amyotrophic lateral sclerosis and tauopathies. Here we uncover that activation of endogenous retroviruses affects prion-like spreading of proteopathic seeds. We show that upregulation of endogenous retroviruses drastically increases the dissemination of protein aggregates between cells in culture, a process that can be inhibited by targeting the viral envelope protein or viral protein processing. Human endogenous retrovirus envelopes of four different clades also elevate intercellular spreading of proteopathic seeds, including pathological Tau. Our data support a role of endogenous retroviruses in protein misfolding diseases and suggest that antiviral drugs could represent promising candidates for inhibiting protein aggregate spreading.
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650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Endogenous Retroviruses: genetics
|2 MeSH
650 _ 2 |a Protein Aggregates
|2 MeSH
650 _ 2 |a Amyotrophic Lateral Sclerosis
|2 MeSH
650 _ 2 |a Antiviral Agents
|2 MeSH
650 _ 2 |a Prions
|2 MeSH
650 _ 7 |a Protein Aggregates
|2 NLM Chemicals
650 _ 7 |a Antiviral Agents
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650 _ 7 |a Prions
|2 NLM Chemicals
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|e Laboratory Automation Technologies (CRFS-LAT) / Bonn
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700 1 _ |a Heumueller, Stefanie-Elisabeth
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700 1 _ |a Hossinger, André
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700 1 _ |a Müller, Stephan A
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700 1 _ |a Buravlova, Oleksandra
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700 1 _ |a Lichtenthaler, Stefan F
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700 1 _ |a Denner, Philip
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700 1 _ |a Vorberg, Ina M
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773 _ _ |a 10.1038/s41467-023-40632-z
|g Vol. 14, no. 1, p. 5034
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|t Nature Communications
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