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000276154 1001_ $$aArshad, Hamza$$b0
000276154 245__ $$aThe brain interactome of a permissive prion replication substrate.
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000276154 520__ $$aBank 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.
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000276154 650_7 $$2Other$$aBank voles
000276154 650_7 $$2Other$$aKnock-in mice
000276154 650_7 $$2Other$$aMass spectrometry
000276154 650_7 $$2Other$$aPrion
000276154 650_7 $$2Other$$aProtein-protein interactions
000276154 7001_ $$aEid, Shehab$$b1
000276154 7001_ $$aMehra, Surabhi$$b2
000276154 7001_ $$aWilliams, Declan$$b3
000276154 7001_ $$0P:(DE-2719)2810486$$aKaczmarczyk, Lech$$b4
000276154 7001_ $$aStuart, Erica$$b5
000276154 7001_ $$0P:(DE-2719)2810253$$aJackson, Walker Scot$$b6
000276154 7001_ $$aSchmitt-Ulms, Gerold$$b7
000276154 7001_ $$aWatts, Joel C$$b8
000276154 773__ $$0PERI:(DE-600)1471408-5$$a10.1016/j.nbd.2025.106802$$gVol. 206, p. 106802 -$$p106802$$tNeurobiology of disease$$v206$$x0969-9961$$y2025
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