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• W2000604385 abstract "ABSTRACT Natural transmission of prion diseases depends upon the spread of prions from the nervous system to excretory or secretory tissues, but the mechanism of prion transport in axons and into peripheral tissue is unresolved. Here, we examined the temporal and spatial movement of prions from the brain stem along cranial nerves into skeletal muscle as a model of axonal transport and transynaptic spread. The disease-specific isoform of the prion protein, PrP Sc , was observed in nerve fibers of the tongue approximately 2 weeks prior to PrP Sc deposition in skeletal muscle. Initially, PrP Sc deposits had a small punctate pattern on the edge of muscle cells that colocalized with synaptophysin, a marker for the neuromuscular junction (NMJ), in >50% of the cells. At later time points PrP Sc was widely distributed in muscle cells, but <10% of prion-infected cells exhibited PrP Sc deposition at the NMJ, suggesting additional prion replication and dissemination within muscle cells. In contrast to the NMJ, PrP Sc was not associated with synaptophysin in nerve fibers but was found to colocalize with LAMP-1 and cathepsin D during early stages of axonal spread. We propose that PrP Sc -bound endosomes can lead to membrane recycling in which PrP Sc is directed to the synapse, where it either moves across the NMJ into the postsynaptic muscle cell or induces PrP Sc formation on muscle cells across the NMJ. IMPORTANCE Prion diseases are transmissible and fatal neurodegenerative diseases in which prion dissemination to excretory or secretory tissues is necessary for natural disease transmission. Despite the importance of this pathway, the cellular mechanism of prion transport in axons and into peripheral tissue is unresolved. This study demonstrates anterograde spread of prions within nerve fibers prior to infection of peripheral synapses (i.e., neuromuscular junction) and infection of peripheral tissues (i.e., muscle cells). Within nerve fibers prions were associated with the endosomal-lysosomal pathway prior to entry into muscle cells. Since early prion spread is anterograde and endosome-lysosomal movement within axons is primarily retrograde, these findings suggest that endosome-bound prions may have an alternate fate that directs prions to the peripheral synapse." @default.
• W2000604385 created "2016-06-24" @default.
• W2000604385 creator A5088835571 @default.
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• W2000604385 date "2014-08-01" @default.
• W2000604385 modified "2023-09-27" @default.
• W2000604385 title "Axonal and Transynaptic Spread of Prions" @default.
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• W2000604385 doi "https://doi.org/10.1128/jvi.00378-14" @default.
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