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Deciphering the prion code

Prions are proteinaceous infectious particles that allow the propagation and inheritance of structural information by proteins. Prions populate the tree of life, propagating as fibrils both in laboratory strains and in the wild. Disease-causing prions are responsible for transmissible spongiform encephalopathies, a wide range of neurodegenerative disorders affecting a variety of species. In humans, prion diseases include fatal familial insomnia, Creutzfeld-Jakob disease, and Kuru. The shape of infectious prions has long been thought to define their infectivity, but remained elusive for decades. My group recently determined the first atomic model of the structured core of a human prion fibril, and with it, unlocked clues to the molecular basis of prion infectivity, transmission and neurotoxicity. Using electron cryo-microscopy (cryoEM) methods, my group pursues structures of a variety of prions including disease-causing human prion variants, infectious prions in related mammals (elk, mouse, bank vole), and functional prions. Our studies aim to establish a rosetta stone for linking prion structure to function and present a starting point to the design of inhibitors or diagnostics that curb the effects of prion disease and offer insights into other amyloid diseases such as Parkinson’s or Alzheimer’s.

Speaker: Jose Rodriguez, UC Los Angeles

Monday, 12/06/21


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Stanley Hall

UC Berkeley
Room 105
Berkeley, CA 94720