Reactivated endogenous retroviruses promote protein aggregate spreading.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 08 2023
18 08 2023
Historique:
received:
21
06
2022
accepted:
02
08
2023
medline:
21
8
2023
pubmed:
19
8
2023
entrez:
18
8
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 37596282
doi: 10.1038/s41467-023-40632-z
pii: 10.1038/s41467-023-40632-z
pmc: PMC10439213
doi:
Substances chimiques
Protein Aggregates
0
Antiviral Agents
0
Prions
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5034Informations de copyright
© 2023. Springer Nature Limited.
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