Prion最新文献

{"title":"Cross-validation of the RT-QuIC assay for the antemortem detection of chronic wasting disease in elk.","authors":"N J Haley,&nbsp;R Donner,&nbsp;D M Henderson,&nbsp;J Tennant,&nbsp;E A Hoover,&nbsp;M Manca,&nbsp;B Caughey,&nbsp;N Kondru,&nbsp;S Manne,&nbsp;A Kanthasamay,&nbsp;S Hannaoui,&nbsp;S C Chang,&nbsp;S Gilch,&nbsp;S Smiley,&nbsp;G Mitchell,&nbsp;A D Lehmkuhl,&nbsp;B V Thomsen","doi":"10.1080/19336896.2020.1716657","DOIUrl":"https://doi.org/10.1080/19336896.2020.1716657","url":null,"abstract":"<p><p>Chronic wasting disease is a progressively fatal, horizontally transmissible prion disease affecting several members of the cervid species. Conventional diagnosis relies on ELISA or IHC evaluation using tissues collected post-mortem; however, recent research has focused on newly developed amplification techniques using samples collected antemortem. The present study sought to cross-validate the real-time quaking-induced conversion assay (RT-QuIC) evaluation of rectal biopsies collected from an elk herd with endemic CWD, assessing both binary positive/negative test results as well as relative rates of amplification between laboratories. We found that results were correlative in both categories across all laboratories performing RT-QuIC, as well as to conventional IHC performed at a national reference laboratory. A significantly higher number of positive samples were identified using RT-QuIC, with results seemingly unhindered by low follicle counts. These findings support the continued development and implementation of amplification assays in the diagnosis of prion diseases of veterinary importance, targeting not just antemortem sampling strategies, but post-mortem testing approaches as well.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":"14 1","pages":"47-55"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1716657","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10764520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"25 years of yeast prions.","authors":"Frank Shewmaker,&nbsp;Dan Masison","doi":"10.1080/19336896.2019.1710420","DOIUrl":"https://doi.org/10.1080/19336896.2019.1710420","url":null,"abstract":"In the early 1990s, Reed Wickner developed a novel hypothesis. For decades it was known that two phenotypes of the yeast Saccharomyces cerevisiae followed non-Mendelian patterns of inheritance [1,2]. These phenotypes were designated [PSI+] and [URE3]. When yeast strains were mated, if either parental strain had one of these phenotypes, all daughter spore clones would inherit the phenotype, although only half would be expected to if the phenotypes were governed by a nuclear gene. Instead, the genetic element resided in the cytoplasm as if it were one of the many yeast viruses. However, unlike yeast viruses, no nucleic acid could be identified. To explain these observations, Reed postulated that the genetic element was composed of protein, not nucleic acid. In 1994, Reed solo-authored an article in Science titled, ‘[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae’, where he described how the puzzling [URE3] and [PSI+] phenotypes could be explained simply as selfpropagating misshapen forms of the Ure2 and Sup35 proteins, respectively [3]. His experiments elegantly demonstrated that the Ure2 protein was itself the critical factor for the formation and propagation of the [URE3] prion, and he proposed that it was a yeast analog of mammalian prions. Noting the logical parallels with [PSI+] and the Sup35 protein, he extended his hypothesis to include [PSI+] as a prion analog of the Sup35 protein, opening the door for discovery of other prions in yeast. At that time, the prion concept – suggesting a form of the protein PrP was the infectious entity responsible for prion disease – was controversial and applied solely to the infectious species that caused transmissible spongiform encephalopathies of mammals (e.g. scrapie, Kuru and Mad Cow disease). Little else was known of PrP extracted from infectious brain aside from it being fibrous aggregates enriched in beta-sheet structure. Whether PrP was a prion component, the prion component, or merely a propagation factor for another pathological agent, was arguable. The question of whether prions existed in nature as defined (i.e. infectious proteins) remained unresolved. The enormous impact of Reed’s short paper is made obvious by the suddenly renewed and widespread interest in non-Mendelian genetic elements and the dramatic evolution of the scientific community’s view of prions in the 25 years since its publication. The broad acceptance of prion mechanisms is largely based on work and ideas pioneered by Reed and colleagues in the yeast model system. These studies provided the first confirmation of protein-only infectious elements and identified a common structural model that enabled a mechanism of protein infectivity: self-propagating amyloid with parallel in-register beta-sheet architecture [4]. This conceptual framework established how prion, or prion-like, mechanisms could be involved in human diseases, especially neurodegenerative disorders that commonly feature pat","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"29-30"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2019.1710420","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37516567","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corticobasal manifestations of Creutzfeldt-Jakob disease with D178N-homozygous 129M genotype.","authors":"Yumeng Huang,&nbsp;Ma Jianfang,&nbsp;Rodrigo Morales,&nbsp;Huidong Tang","doi":"10.1080/19336896.2020.1812367","DOIUrl":"https://doi.org/10.1080/19336896.2020.1812367","url":null,"abstract":"<p><p>Creutzfeldt-Jakob disease (CJD) is a prion disease, usually presented with memory loss, ataxia, dementia, myoclonus, involuntary movements and psychiatric problems. D178N-homozygous 129M genotype has been recognized in the diagnosis of fatal familial insomnia (FFI) globally. Here we report a patient presented with progressive left upper limb stiffness, bradykinesia, hypomimia and weight loss (10 kg) initially. She progressed to dementia, dysphasia, dysphonia and be bedridden quickly but did not present insomnia. She was diagnosed with CJD corticobasal subtype carrying a classic D178N-129M mutation of <i>PRNP</i> in FFI. Remarkably, she has a strong family history of neurological degeneration diseases but the other members of this pedigree who do not carry D178N-homozygous 129M mutation in <i>PRNP</i> do not present any CJD or FFI symptoms. We conclude that this patient carrying D178N-homozygous 129M mutation in <i>PRNP</i> should be diagnosed as CJD. Thus, the clinicopathology should be considered as a crucial evidence in diagnosing some cases, but FFI could be evaluated as a differential diagnosis with a unique clinical profile. <b>List of abbreviations</b> AD: Alzheimer disease; ADL: Activities of Daily Living; CBD Cortical basal degeneration; CBS: Corticobasal syndrome; CJD: Creutzfeldt-Jakob disease; DWI: Diffusion-weighted image; EEG: Electroencephalograph, fCJD: familial Creutzfeld-Jakob disease; FFI: Fatal familial insomnia; FLAIR: Fluid-attenuated inversion recovery; MMSE: Mini-mental state examination; MoCA: Montreal Cognitive Assessment; MRI: Magnetic resonance imaging; PD: Parkinson disease; PrP: Prion protein; PSWC: Periodic sharp wave complexes; SWI: Susceptibility-weighted imaging.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"232-237"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1812367","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38393517","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rare genetic E196A mutation in a patient with Creutzfeldt-Jakob disease: a case report and literature.","authors":"Xiping Wu,&nbsp;Zhao Cui,&nbsp;Xie Guomin,&nbsp;Haifeng Wang,&nbsp;Xiaoling Zhang,&nbsp;Zhiguang Li,&nbsp;Qi Sun,&nbsp;Feiteng Qi","doi":"10.1080/19336896.2020.1769528","DOIUrl":"https://doi.org/10.1080/19336896.2020.1769528","url":null,"abstract":"<p><p>Genetic Creutzfeldt-Jakob disease (gCJD) is characterized by mutations in the PRNP gene and represents approximately 10-15% of the human prion diseases. Here, we report a 42-year-old Chinese man who was diagnosed with gCJD. The patient had a rare mutation in codon 196 (E196A) of PRNP leading to an exchange of amino acid from glutamic acid (E) to alanine (A). The polymorphism of codon 129 in the patient was methionine homozygote. His mother and daughter are asymptomatic carriers of the same mutation. The clinical manifestations were similar to those of sporadic CJD. 14-3-3 protein was positive in cerebrospinal fluid, and there were sharp slow complex waves in electroencephalography and ribbon-like signals on magnetic resonance imaging (MRI). The main complaints of patient changed from visual space and visual colour to psychotic symptoms with enhanced high signal intensity on the occipital and frontal cortices on MRI. We compared the clinical characteristics of the current patient with those of previously reported Chinese patients with other gCJD of E196A mutation to summarize the common features of E196A gCJD.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"143-148"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1769528","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38014521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"RT-QuIC-based detection of alpha-synuclein seeding activity in brains of dementia with Lewy Body patients and of a transgenic mouse model of synucleinopathy.","authors":"Jung-Youn Han, Hyung-Sup Jang, Alison J E Green, Young Pyo Choi","doi":"10.1080/19336896.2020.1724608","DOIUrl":"10.1080/19336896.2020.1724608","url":null,"abstract":"<p><p>RT-QuIC is a shaking-based cyclic amplification technique originally developed in the prion field to detect minute amounts of scrapie prion protein (PrP^Sc). In this study, we applied the RT-QuIC assay to investigate a-synuclein (a-syn) seeding activity in brains of Dementia with Lewy Body (DLB) patients and in brains of G2-3 transgenic mice expressing human a-syn with A53T mutation. The results show that a-syn seeding activity varies between patients with detectable dilutions ranging from 10^-3 to 10^-8 dilutions of brain tissue and is stable under exposures to the cycles of freezing, thawing and sonication. A53T a-syn aggregates from G2-3 transgenic mice greatly favoured A53T recombinant human a-syn as substrates in comparison to wild-type a-syn, suggesting that conformations for wild-type a-syn to be able to adopt are not compatible with that of A53T aggregates from G2-3.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"88-94"},"PeriodicalIF":1.9,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7039666/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37628646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Management of chronic wasting disease in ranched elk: conclusions from a longitudinal three-year study.","authors":"N J Haley,&nbsp;D M Henderson,&nbsp;R Donner,&nbsp;S Wyckoff,&nbsp;K Merrett,&nbsp;J Tennant,&nbsp;E A Hoover,&nbsp;D Love,&nbsp;E Kline,&nbsp;A D Lehmkuhl,&nbsp;B V Thomsen","doi":"10.1080/19336896.2020.1724754","DOIUrl":"https://doi.org/10.1080/19336896.2020.1724754","url":null,"abstract":"<p><p>Chronic wasting disease is a fatal, horizontally transmissible prion disease of cervid species that has been reported in free-ranging and farmed animals in North America, Scandinavia, and Korea. Like other prion diseases, CWD susceptibility is partly dependent on the sequence of the prion protein encoded by the host's <i>PRNP</i> gene; it is unknown if variations in <i>PRNP</i> have any meaningful effects on other aspects of health. Conventional diagnosis of CWD relies on ELISA or IHC testing of samples collected post-mortem, with recent efforts focused on antemortem testing approaches. We report on the conclusions of a study evaluating the role of antemortem testing of rectal biopsies collected from over 570 elk in a privately managed herd, and the results of both an amplification assay (RT-QuIC) and conventional IHC among animals with a several <i>PRNP</i> genotypes. Links between <i>PRNP</i> genotype and potential markers of evolutionary fitness, including pregnancy rates, body condition, and annual return rates were also examined. We found that the RT-QuIC assay identified significantly more CWD positive animals than conventional IHC across the course of the study, and was less affected by factors known to influence IHC sensitivity - including follicle count and PRNP genotype. We also found that several evolutionary markers of fitness were not adversely correlated with specific <i>PRNP</i> genotypes. While the financial burden of the disease in this herd was ultimately unsustainable for the herd owners, our scientific findings and the hurdles encountered will assist future CWD management strategies in both wild and farmed elk and deer.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":"14 1","pages":"76-87"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1724754","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10764522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils.","authors":"M I Sulatsky,&nbsp;A I Sulatskaya,&nbsp;O I Povarova,&nbsp;Iu A Antifeeva,&nbsp;I M Kuznetsova,&nbsp;K K Turoverov","doi":"10.1080/19336896.2020.1720487","DOIUrl":"https://doi.org/10.1080/19336896.2020.1720487","url":null,"abstract":"<p><p>Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"67-75"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1720487","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37601796","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Serial evaluation of swallowing function in a long-term survivor of V180I genetic Creutzfeldt-Jakob disease.","authors":"Kenjiro Kunieda,&nbsp;Yuichi Hayashi,&nbsp;Megumi Yamada,&nbsp;Masahiro Waza,&nbsp;Tomonori Yaguchi,&nbsp;Ichiro Fujishima,&nbsp;Takayoshi Shimohata","doi":"10.1080/19336896.2020.1787090","DOIUrl":"https://doi.org/10.1080/19336896.2020.1787090","url":null,"abstract":"<p><p>Swallowing function in long-term survivors with Creutzfeldt-Jakob disease (CJD) remains unknown. Herein, we demonstrated serial evaluation of swallowing function in a case with V180I genetic CJD (gCJD) using videofluoroscopic examination of swallowing (VF). A 69-year-old woman was admitted to our hospital because of bradykinesia and memory disturbances 4 months after the onset of symptoms. Neurological examination revealed dementia, bradykinesia and frontal signs. Diffusion-weighted MRI revealed bilateral cortical hyperintensity in the frontal, temporal, and parietal cortices, and <i>PRNP</i> gene analysis indicated a V180I mutation. Her dysphagia gradually progressed, and she received percutaneous gastrostomy 42 months after the onset. VF was performed at 27, 31, 39, and 79 months after the onset. Although bolus transport from oral cavity to pharynx gradually worsened and initiation of the pharyngeal swallow was gradually delayed, the pharyngeal swallowing function was preserved even at 72 months after onset. MRI revealed no apparent atrophy of brainstem, and single photon emission computed tomography showed preserved regional cerebral blood flow in the brainstem. These findings suggest that the pathophysiology of dysphagia in a long-term survivor of V180I gCJD is that of pseudobulbar palsy, likely owing to preserved brainstem function even in the akinetic mutism state.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"180-184"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1787090","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38122959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Estimation of amyloid aggregate sizes with semi-denaturing detergent agarose gel electrophoresis and its limitations.","authors":"Polina B Drozdova,&nbsp;Yury A Barbitoff,&nbsp;Mikhail V Belousov,&nbsp;Rostislav K Skitchenko,&nbsp;Tatyana M Rogoza,&nbsp;Jeremy Y Leclercq,&nbsp;Andrey V Kajava,&nbsp;Andrew G Matveenko,&nbsp;Galina A Zhouravleva,&nbsp;Stanislav A Bondarev","doi":"10.1080/19336896.2020.1751574","DOIUrl":"https://doi.org/10.1080/19336896.2020.1751574","url":null,"abstract":"<p><p>Semi-denaturing detergent agarose gel electrophoresis (SDD-AGE) was proposed by Vitaly V. Kushnirov in the Michael D. Ter-Avanesyan's laboratory as a method to compare sizes of amyloid aggregates. Currently, this method is widely used for amyloid investigation, but mostly as a qualitative approach. In this work, we assessed the possibilities and limitations of the quantitative analysis of amyloid aggregate size distribution using SDD-AGE results. For this purpose, we used aggregates of two well-characterized yeast amyloid-forming proteins, Sup35 and Rnq1, and developed a protocol to standardize image analysis and process the result. A detailed investigation of factors that may affect the results of SDD-AGE revealed that both the cell lysis method and electrophoresis conditions can substantially affect the estimation of aggregate size. Despite this, quantitative analysis of SDD-AGE results is possible when one needs to estimate and compare the size of aggregates on the same gel, or even in different experiments, if the experimental conditions are tightly controlled and additional standards are used.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"118-128"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1751574","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37847681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of Chinese patients with sporadic Creutzfeldt-Jakob disease.","authors":"Jing Yang,&nbsp;Haiyan Kuang,&nbsp;Qiong Wang,&nbsp;Jiao Liu,&nbsp;Xueping Chen,&nbsp;Huifang Shang","doi":"10.1080/19336896.2020.1761515","DOIUrl":"https://doi.org/10.1080/19336896.2020.1761515","url":null,"abstract":"<p><p>Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare, incurable, and fatal neurodegenerative disorder. The objective of this study was to describe the clinical features and survival time of Chinese sCJD patients, and to explore the associations between clinical data and survival. In this study, we analysed the clinical data of 21 sCJD patients in a tertiary care hospital and used all Chinese case material available from 152 patients with sCJD in literatures between 2008 and 2018. The mean age of onset of all 173 deceased patients was 61.44 year-olds (y), with the highest incidence in the population of 60 to 69 y. The most common manifestation at disease onset was progressive dementia. With the progression of the disease, the four main clinical symptoms and signs were developed, including myoclonus, visual or cerebella disturbance, pyramidal or extrapyramidal dysfunction, and akinetic mutism. Extrapyramidal symptoms were more frequently observed. The mean survival time was 7.34 months, and 82.10% of cases died within 1 year after disease onset. The follow-up showed that the survival time was longer and the myoclonus sign was more frequently presented in younger-onset sCJD patients. Patients with abnormalities only in cortical regions had a higher frequency of pyramidal dysfunction than patients having lesions in both cortex and basal ganglia. The findings of this study might provide some insight into the clinical characteristics of sCJD patients in China, but further studies could examine the presences of clinical features and survival time in patients with early age of onset in a prospective manner.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":" ","pages":"137-142"},"PeriodicalIF":2.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2020.1761515","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37909265","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}