A normal prion protein ($$PrP^C$$) in a cell can be converted into its infectious, misfolded rogue form ($$PrP^{Sc}$$) due to a genetic mutation or spontaneous event. Once formed, the rogue prion protein ($$PrP^{Sc}$$) interacts with and stimulates normal endogenous $$PrP^C$$ proteins to misfold, leading to the accumulation of plaque-like aggregates in nervous tissue.

University of Wisconsin - Madison

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Prions are acellular, infectious protein particles that do not contain DNA or RNA, cause transmissible spongiform encephalopathies, and are excluded from the tree of life. They are exceptionally small, measuring approximately $${}1/10$$ the size of a typical virus, and are extremely resistant to heat, chemicals, and radiation. Currently, there is no treatment or cure for prion infections.

Prions

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Microbiology covers the scope and sequence requirements for a single-semester microbiology course for non-majors. The book presents the core concepts of microbiology with a focus on applications for careers in allied health. The pedagogical features of the text make the material interesting and accessible while maintaining the career-application focus and scientific rigor inherent in the subject matter. Microbiology’s art program enhances students’ understanding of concepts through clear and effective illustrations, diagrams, and photographs.

Microbiology is produced through a collaborative publishing agreement between OpenStax and the American Society for Microbiology Press. The book aligns with the curriculum guidelines of the American Society for Microbiology.

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Prion Misfolding and Disease Onset

Symptoms of transmissible spongiform encephalopathies (TSE) include severe brain damage, loss of motor coordination, dementia, and mental impairment. As the disease rapidly progresses, affected individuals become completely unable to move or speak, eventually leading to death.

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