Journal Article

DZNE-2025-00226

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The brain interactome of a permissive prion replication substrate.

Arshad, H. ; Eid, S. ; Mehra, S. ; Williams, D. ; Kaczmarczyk, L.DZNE* ; Stuart, E. ; Jackson, W. S.DZNE* ; Schmitt-Ulms, G. ; Watts, J. C.

2025
Elsevier [Amsterdam]

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Please use a persistent id in citations: doi:10.1016/j.nbd.2025.106802

Abstract: Bank voles are susceptible to prion strains from many different species, yet the molecular mechanisms underlying the ability of bank vole prion protein (BVPrP) to function as a universal prion acceptor remain unclear. Potential differences in molecular environments and protein interaction networks on the cell surface of brain cells may contribute to BVPrP's unusual behavior. To test this hypothesis, we generated knock-in mice that express physiological levels of BVPrP (M109 isoform) and employed mass spectrometry to compare the interactomes of mouse (Mo) PrP and BVPrP following mild in vivo crosslinking of brain tissue. Substantial overlap was observed between the top interactors for BVPrP and MoPrP, with established PrP-interactors such as neural cell adhesion molecules, subunits of Na+/K+-ATPases, and contactin-1 being equally present in the two interactomes. We conclude that the molecular environments of BVPrP and MoPrP in the brains of mice are very similar. This suggests that the unorthodox properties of BVPrP are unlikely to be mediated by differential interactions with other proteins.

Keyword(s): Bank voles ; Knock-in mice ; Mass spectrometry ; Prion ; Protein-protein interactions

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Contributing Institute(s):

1. Selective Vulnerability of Neurodegenerative Diseases (AG Jackson)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)

Appears in the scientific report 2025

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