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Infectious Prions Accumulate to High Levels in Non Proliferative C2C12 Myotubes
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نویسنده
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herbst a. ,banser p. ,velasquez c.d. ,mays c.e. ,sim v.l. ,westaway d. ,aiken j.m. ,mckenzie d.
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منبع
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plos pathogens - 2013 - دوره : 9 - شماره : 11
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چکیده
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Prion diseases are driven by the strain-specific,template-dependent transconformation of the normal cellular prion protein (prpc) into a disease specific isoform prpsc. cell culture models of prion infection generally use replicating cells resulting in lower levels of prion accumulation compared to animals. using non-replicating cells allows the accumulation of higher levels of prpsc and,thus,greater amounts of infectivity. here,we infect non-proliferating muscle fiber myotube cultures prepared from differentiated myoblasts. we demonstrate that prion-infected myotubes generate substantial amounts of prpsc and that the level of infectivity produced in these post-mitotic cells,105.5 l.d.50/mg of total protein,approaches that observed in vivo. exposure of the myotubes to different mouse-adapted agents demonstrates strain-specific replication of infectious agents. mouse-derived myotubes could not be infected with hamster prions suggesting that the species barrier effect is intact. we suggest that non-proliferating myotubes will be a valuable model system for generating infectious prions and for screening compounds for anti-prion activity. © 2013 herbst et al.
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آدرس
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centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,department of agriculture,food and nutritional sciences,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,department of biological sciences,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,department of agriculture,food and nutritional sciences,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,division of neuroscience,department of medicine,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,division of neuroscience,department of medicine,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,division of neuroscience,department of medicine,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,department of agriculture,food and nutritional sciences,university of alberta,edmonton,ab, Canada, centre for prions and protein folding diseases,university of alberta,edmonton,ab,canada,department of biological sciences,university of alberta,edmonton,ab, Canada
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Authors
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