title: The transcellular spread of cytosolic amyloids, prions, and prionoids.
abstract: Recent reports indicate that a growing number of intracellular proteins are not only prone to pathological aggregation but can also be released and "infect" neighboring cells. Therefore, many complex diseases may obey a simple model of propagation where the penetration of seeds into hosts determines spatial spread and disease progression. We term these proteins prionoids, as they appear to infect their neighbors just like prions--but how can bulky protein aggregates be released from cells and how do they access other cells? The widespread existence of such prionoids raises unexpected issues that question our understanding of basic cell biology.
authors.affiliation: Institute of Neuropathology, University Hospital of Zürich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland. adriano.aguzzi@usz.ch
authors.forename: Adriano
authors.initials: A
authors.lastname: Aguzzi
authors.forename: Lawrence
authors.initials: L
authors.lastname: Rajendran
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002450:Cell Communication / Q000502:physiology; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D003600:Cytosol / Q000737:chemistry / Q000378:metabolism; D018562:Disease Transmission, Infectious; D004705:Endocytosis / Q000502:physiology; D005089:Exocytosis / Q000502:physiology; D006801:Humans; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism* / Q000503:physiopathology; D011328:Prions / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport / Q000502:physiology
chemical_list: D000682:Amyloid; D011328:Prions