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Prion disease in Indigenous Australians.

土著澳大利亚人的朊病毒病。

  • 影响因子:1.21
  • DOI:10.1111/imj.14835
  • 作者列表:"Panegyres PK","Stehmann C","Klug GM","Masters CL","Collins S
  • 发表时间:2020-04-01
Abstract

BACKGROUND:Indigenous Australians are of increased risk of developing dementia - Alzheimer's disease and mixed dementia diagnoses are the most common. Whilst prion diseases have been reported in Indigenous peoples of Papua New Guinea and the United States of America, the occurrence and phenotype of prion disease in Indigenous Australians is hitherto unreported. AIM:Report the incidence rate and clinical phenotype of Creutzfeldt-Jakob disease (CJD) in Indigenous Australians. METHOD:Calculation of crude sporadic CJD (sCJD) incidence rates and indirect age-standardisation of all CJD to calculate the standardised mortality ratio (SMR) for the Indigenous Australian population in comparison to the all-resident Australian population, along with analysis of clinical phenotype. RESULTS:Illustrative case report of an Indigenous Australian from regionally remote Western Australia dying from typical "probable "sCJD two months after disease onset, with Australian National CJD Registry (ANCJDR) surveillance overall ascertaining eight Indigenous Australians dying from sCJD (5 post-mortem confirmed, 3 classified as "probable") with the clinical phenotype similar to non-Indigenous people, including median age at death of 61 years (interquartile range IQR = 16 years) and median duration of illness 3 months (IQR = 1.6 months). Indigenous Australians with sCJD were geographically dispersed throughout Australia. The calculated overall crude annual rate of sCJD in Indigenous Australians compared to the remainder of the Australian population was not significantly different (0-3.87/million for Indigenous Australians; 0.94-1.83/million for non-Indigenous). The indirect age-standardised all CJD mortality ratio for the Indigenous population for the years 2006 to 2018 was 1.49 (95% CI, 0.75-2.98), also not significantly different to the all-resident Australian population. CONCLUSION:CJD occurs in Indigenous Australians with the clinical phenotype and occurrence rates similar to non-Indigenous Australians. These findings contrast with a previous report wherein the incidence rate of CJD in a non-Australian Indigenous populations was reported as decreased. This article is protected by copyright. All rights reserved.

摘要

背景: 澳大利亚土著居民患痴呆的风险增加 -- 阿尔茨海默病和混合痴呆的诊断是最常见的。虽然在巴布亚新几内亚和美利坚合众国的土著人民中报告了朊病毒病,但土著澳大利亚人中朊病毒病的发生和表型迄今尚未报告。 目的: 报道澳大利亚土著居民克雅氏病 (CJD) 的发病率和临床表型。 方法: 计算所有 CJD 的粗散发性 CJD (sCJD) 发病率和间接年龄标准化,以计算标准化死亡率比 (SMR) 对于澳大利亚土著人口与全居民澳大利亚人口的比较,以及临床表型的分析。 结果: 澳大利亚国家 CJD 登记处 (ANCJDR) 在疾病发作后两个月死于典型 “可能” sCJD 的澳大利亚土著居民的说明性病例报告监测总体确定 8 名澳大利亚土著居民死于 sCJD (5 例尸检证实,3 例归类为 “可能”)临床表型与非土著人相似,包括死亡时的中位年龄 61 岁 (四分位距 IQR = 16 岁) 中位病程 3 个月 (IQR = 1.6 个月)。患有 sCJD 的土著澳大利亚人在地理上分散在整个澳大利亚。计算的土著澳大利亚人 sCJD 的总体粗年增长率与其余澳大利亚人口相比没有显著差异 (土著澳大利亚人为 0-3.87/百万; 0.94-1.83/百万,非土著)。2006年至 2018年土著人口的间接年龄标准化 all CJD 死亡率比为 1.49 (95% CI,0.75-2.98),与全澳大利亚常住人口也无显著差异。 结论: CJD 发生于土著澳大利亚人,其临床表型和发生率与非土著澳大利亚人相似。这些发现与之前的报告相反,其中非澳大利亚土著居民中 CJD 的发病率报告为下降。本文受版权保护。保留所有权利。

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相关文献
影响因子:3.85
发表时间:2020-01-14
来源期刊:Neurology
DOI:10.1212/WNL.0000000000008680
作者列表:["Maddox RA","Person MK","Blevins JE","Abrams JY","Appleby BS","Schonberger LB","Belay ED"]

METHODS:OBJECTIVE:To report the incidence of prion disease in the United States. METHODS:Prion disease decedents were retrospectively identified from the US national multiple cause-of-death data for 2003-2015 and matched with decedents in the National Prion Disease Pathology Surveillance Center (NPDPSC) database through comparison of demographic variables. NPDPSC decedents with neuropathologic or genetic test results positive for prion disease for whom no match was found in the multiple cause-of-death data were added as cases for incidence calculations; those with cause-of-death data indicating prion disease but with negative neuropathology results were removed. Age-specific and age-adjusted average annual incidence rates were then calculated. RESULTS:A total of 5,212 decedents were identified as having prion disease, for an age-adjusted average annual incidence of 1.2 cases per million population (range 1.0 per million [2004 and 2006] to 1.4 per million [2013]). The median age at death was 67 years. Ten decedents were <30 years of age (average annual incidence of 6.2 per billion); only 2 of these very young cases were sporadic forms of prion disease. Average annual incidence among those ≥65 years of age was 5.9 per million. CONCLUSIONS:Prion disease incidence can be estimated by augmenting mortality data with the results of neuropathologic and genetic testing. Cases <30 years of age were extremely rare, and most could be attributed to exogenous factors or the presence of a genetic mutation. Continued vigilance for prion diseases in all age groups remains prudent.

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影响因子:2.78
发表时间:2020-01-08
DOI:10.1080/07391102.2019.1708794
作者列表:["Soto P","Claflin IA","Bursott AL","Schwab-McCoy AD","Bartz JC"]

METHODS::The conformational conversion of the cellular prion protein (PrPC) to the misfolded and aggregated isoform, termed scrapie prion protein (PrPSc), is key to the development of a group of neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). Although the conversion mechanism is not fully understood, the role of gene polymorphisms in varying susceptibilities to prion diseases is well established. In ovine, specific gene polymorphisms in PrPC alter prion disease susceptibility: the Valine136-Glutamine171 variant (Susceptible structure) displays high susceptibility to classical scrapie while the Alanine136-Arginine171 variant (Resistant structure) displays reduced susceptibility. The opposite trend has been reported in atypical scrapie. Despite the differentiation between classical and atypical scrapie, a complete understanding of the effect of polymorphisms on the structural dynamics of PrPC is lacking. From our structural bioinformatics study, we propose that polymorphisms locally modulate the network of residue interactions in the globular C-terminus of the ovine recombinant prion protein while maintaining the overall fold. Although the two variants we examined exhibit a densely connected group of residues that includes both β-sheets, the β2-α2 loop and the N-terminus of α-helix 2, only in the Resistant structure do most residues of α-helix 2 belong to this group. We identify the structural role of Valine136Alanine and Glutamine171Arginine: modulation of residue interaction networks that affect the connectivity between α-helix 2 and α-helix 3. We propose blocking interactions of residue 171 as a potential target for the design of therapeutics to prevent efficient PrPC misfolding. We discuss our results in the context of initial PrPC conversion and extrapolate to recently proposed PrPSc structures.Communicated by Ramaswamy H. Sarma.

影响因子:4.10
发表时间:2020-01-09
DOI:10.1093/infdis/jiz646
作者列表:["Espinosa JC","Marín-Moreno A","Aguilar-Calvo P","Benestad SL","Andreoletti O","Torres JM"]

METHODS::Although experimental transmission of bovine spongiform encephalopathy (BSE) to pigs and transgenic mice expressing pig cellular prion protein (PrPC) (porcine PrP [PoPrP]-Tg001) has been described, no natural cases of prion diseases in pig were reported. This study analyzed pig-PrPC susceptibility to different prion strains using PoPrP-Tg001 mice either as animal bioassay or as substrate for protein misfolding cyclic amplification (PMCA). A panel of isolates representatives of different prion strains was selected, including classic and atypical/Nor98 scrapie, atypical-BSE, rodent scrapie, human Creutzfeldt-Jakob-disease and classic BSE from different species. Bioassay proved that PoPrP-Tg001-mice were susceptible only to the classic BSE agent, and PMCA results indicate that only classic BSE can convert pig-PrPC into scrapie-type PrP (PrPSc), independently of the species origin. Therefore, conformational flexibility constraints associated with pig-PrP would limit the number of permissible PrPSc conformations compatible with pig-PrPC, thus suggesting that pig-PrPC may constitute a paradigm of low conformational flexibility that could confer high resistance to the diversity of prion strains.

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