Genetic Creutzfeldt–Jakob disease‐M232R with the cooccurrence of multiple prion strains, M1 +  M2C +  M2T : Report of an autopsy case

2021 ◽  
Author(s):  
Masayuki Shintaku ◽  
Takeshi Nakamura ◽  
Daita Kaneda ◽  
Akiyo Shinde ◽  
Hirofumi Kusaka ◽  
...  
Keyword(s):  
Autopsy Case ◽  
Prion Strains ◽  
Jakob Disease

An autopsy case of Creutzfeldt-Jakob disease with a V180I mutation of the PrP gene and Alzheimer-type pathology

2010 ◽  
Vol 30 (2) ◽  
pp. 159-164 ◽  
Author(s):  
Hidenori Yoshida ◽  
Seishi Terada ◽  
Hideki Ishizu ◽  
Kenji Ikeda ◽  
Toshiyuki Hayabara ◽  
...  
Keyword(s):  
Autopsy Case ◽  
Alzheimer Type ◽  
Jakob Disease ◽  
Prp Gene

scholarly journals Neuroinvasion in Prion Diseases: The Roles of Ascending Neural Infection and Blood Dissemination

2010 ◽  
Vol 2010 ◽  
pp. 1-16 ◽  
Author(s):  
Sílvia Sisó ◽  
Lorenzo González ◽  
Martin Jeffrey
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Prion Protein ◽  
Prion Diseases ◽  
Autonomic Nerves ◽  
Peripheral Organs ◽  
Prion Strains ◽  
New Variant ◽  
Jakob Disease ◽  
The Central Nervous System

Prion disorders are infectious, neurodegenerative diseases that affect humans and animals. Susceptibility to some prion diseases such as kuru or the new variant of Creutzfeldt-Jakob disease in humans and scrapie in sheep and goats is influenced by polymorphisms of the coding region of the prion protein gene, while other prion disorders such as fatal familial insomnia, familial Creutzfeldt-Jakob disease, or Gerstmann-Straussler-Scheinker disease in humans have an underlying inherited genetic basis. Several prion strains have been demonstrated experimentally in rodents and sheep. The progression and pathogenesis of disease is influenced by both genetic differences in the prion protein and prion strain. Some prion diseases only affect the central nervous system whereas others involve the peripheral organs prior to neuroinvasion. Many experiments undertaken in different species and using different prion strains have postulated common pathways of neuroinvasion. It is suggested that prions access the autonomic nerves innervating peripheral organs and tissues to finally reach the central nervous system. We review here published data supporting this view and additional data suggesting that neuroinvasion may concurrently or independently involve the blood vascular system.

scholarly journals Analysis of Prion Strains by PrPSc Profiling in Sporadic Creutzfeldt–Jakob Disease

PLoS Medicine ◽  
2005 ◽  
Vol 3 (2) ◽  
pp. e14 ◽  
Author(s):  
Gaby Schoch ◽  
Harald Seeger ◽  
Julien Bogousslavsky ◽  
Markus Tolnay ◽  
Robert Charles Janzer ◽  
...  
Keyword(s):  
Prion Strains ◽  
Jakob Disease

Biochemical and conformational variability of human prion strains in sporadic Creutzfeldt–Jakob disease

1999 ◽  
Vol 274 (1) ◽  
pp. 33-36 ◽  
Author(s):  
Pierre Aucouturier ◽  
Richard J Kascsak ◽  
Blas Frangione ◽  
Thomas Wisniewski
Keyword(s):  
Conformational Variability ◽  
Prion Strains ◽  
Jakob Disease

scholarly journals Correction: Regulating Factors of PrPres Glycosylation in Creutzfeldt-Jakob Disease - Implications for the Dissemination and the Diagnosis of Human Prion Strains

PLoS ONE ◽  
2008 ◽  
Vol 3 (9) ◽  
Author(s):  
Etienne Levavasseur ◽  
Isabelle Laffont-Proust ◽  
Émilie Morain ◽  
Baptiste A. Faucheux ◽  
Nicolas Privat ◽  
...  
Keyword(s):  
Prion Strains ◽  
Jakob Disease

scholarly journals AN AUTOPSY CASE OF CREUTZFELDT-JAKOB DISEASE

1981 ◽  
Vol 31 (5) ◽  
pp. 363-372
Author(s):  
SHIGERU TAKAHASHI ◽  
KAZUO MIYANAGA ◽  
MINORU FUKUDA ◽  
KENICHI ISAKA ◽  
TADAKATSU TAKAGI
Keyword(s):  
Autopsy Case ◽  
Jakob Disease

AN AUTOPSY CASE OF CREUTZFELDT-JAKOB DISEASE WITH KURU-LIKE NEUROPATHOLOGICAL CHANGES

1977 ◽  
Vol 27 (2) ◽  
pp. 231-238
Author(s):  
Toru Hirano ◽  
Hideo Tsuchiyama ◽  
Kioko Kawai ◽  
Kazutake Mori
Keyword(s):  
Autopsy Case ◽  
Jakob Disease

scholarly journals Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM

2021 ◽  
Author(s):  
Li-Qiang Wang ◽  
Kun Zhao ◽  
Han-Ye Yuan ◽  
Xiang-Ning Li ◽  
Hai-Bin Dang ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Prion Diseases ◽  
Conformational Stability ◽  
Salt Bridges ◽  
Wild Type ◽  
Left Handed ◽  
Prion Strains ◽  
Fibril Structure ◽  
Clinical Syndromes ◽  
Jakob Disease

Prion diseases are caused by the conformational conversion of prion protein (PrP) from its cellular form (PrPC) into a protease-resistant, aggregated form (PrPSc). 42 different familial mutations were identified in human PrP, which lead to genetic prion diseases with distinct clinical syndromes. Here we report cryo-EM structure of an amyloid fibril formed by full-length human PrP with E196K mutation, a familial Creutzfeldt-Jakob disease-related mutation. This mutation disrupts key interactions in wild-type PrP fibril and results in a rearrangement of the overall structure, forming an amyloid fibril with a conformation distinct from wild-type PrP fibril. The E196K fibril consists of two protofibrils intertwined into a left-handed helix. Each subunit forms five β-strands stabilized by a disulfide bond and an unusual hydrophilic cavity. Two pairs of amino acids (Lys194 and Glu207; Lys196 and Glu200) from opposing subunits form four salt bridges to stabilize the zigzag interface of the two protofibrils. Furthermore, the E196K fibril exhibits a significantly lower conformational stability and protease resistance activity than the wild-type fibril. Our results provide direct structural evidences of the diverse mammalian prion strains and fibril polymorphism of PrP, and highlight the importance of familial mutations in determining the different prion strains.

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