Pub Date : 2024-12-01Epub Date: 2024-05-09DOI: 10.1080/19336896.2024.2349011
Pavol Skacik, Egon Kurca, Stefan Sivak
Authors are commenting on the evolving geographical incidence trends observed with the genetic form of Creutzfeldt-Jakob disease and discussing the diverse array of factors contributing to the heightened incidence rates observed in specific geographical regions.
{"title":"Exploring CJD incidence trends: insights from Slovakia.","authors":"Pavol Skacik, Egon Kurca, Stefan Sivak","doi":"10.1080/19336896.2024.2349011","DOIUrl":"10.1080/19336896.2024.2349011","url":null,"abstract":"<p><p>Authors are commenting on the evolving geographical incidence trends observed with the genetic form of Creutzfeldt-Jakob disease and discussing the diverse array of factors contributing to the heightened incidence rates observed in specific geographical regions.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11085948/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140900290","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}
Pub Date : 2024-12-01Epub Date: 2024-02-07DOI: 10.1080/19336896.2024.2311950
Urwah Rasheed, Sana Khan, Minahil Khalid, Aneeqa Noor, Saima Zafar
Creutzfeldt Jakob Disease (CJD) is a rapidly progressive, fatal neurodegenerative disorder, also known as a subacute spongiform encephalopathy. There are three major subtypes of CJD i.e. Sporadic CJD, which occurs for reasons unbeknown to science (85% of known cases), Genetic or Familial CJD which is characterized by the presence of mutations in the human prion protein (PRNP) gene (10-15% cases) and Iatrogenic CJD that occurs via accidental transmission through medical and surgical procedures (1-2% cases). CJD cases occur globally with 1 case per one million population/year. Considerable data is available related to the incidence and prevalence of CJD in Europe and America. However, the global surveillance database is yet to include Asia even though several Asian countries have their own CJD monitoring units. sCJD is the highest among all CJD cases in Asia. China (1957) and Japan (1705) have reported more cases of sCJD than any Asian country and Hong Kong (1) has reported the least. On the other hand, gCJD is highest in Japan (370) and least in India (2). Our analysis establishes the presence of all variants of CJD across Asia. However, in most Asian countries in general and Southeast Asian countries in particular, CJD cases are misdiagnosed and often underreported. Since Asia is the most populated continent in the world, the actual global prevalence of CJD cannot be estimated until and unless these countries are accounted for. Concrete and reliable surveillance networks are needed across Asia to evaluate the prevalence and incidence of CJD in the region. [Figure: see text]The graphical abstract demonstrates the prevalence of CJD cases in the world and systematically analyses the incidence of CJD in Asian countries between the year 1986-2022. Highest number of cases were reported in Japan followed by China. The study emphasizes the need for assimilation of Asian data in global prevalence.
{"title":"A systemic analysis of Creutzfeldt Jakob disease cases in Asia.","authors":"Urwah Rasheed, Sana Khan, Minahil Khalid, Aneeqa Noor, Saima Zafar","doi":"10.1080/19336896.2024.2311950","DOIUrl":"10.1080/19336896.2024.2311950","url":null,"abstract":"<p><p>Creutzfeldt Jakob Disease (CJD) is a rapidly progressive, fatal neurodegenerative disorder, also known as a subacute spongiform encephalopathy. There are three major subtypes of CJD i.e. Sporadic CJD, which occurs for reasons unbeknown to science (85% of known cases), Genetic or Familial CJD which is characterized by the presence of mutations in the human prion protein (PRNP) gene (10-15% cases) and Iatrogenic CJD that occurs via accidental transmission through medical and surgical procedures (1-2% cases). CJD cases occur globally with 1 case per one million population/year. Considerable data is available related to the incidence and prevalence of CJD in Europe and America. However, the global surveillance database is yet to include Asia even though several Asian countries have their own CJD monitoring units. sCJD is the highest among all CJD cases in Asia. China (1957) and Japan (1705) have reported more cases of sCJD than any Asian country and Hong Kong (1) has reported the least. On the other hand, gCJD is highest in Japan (370) and least in India (2). Our analysis establishes the presence of all variants of CJD across Asia. However, in most Asian countries in general and Southeast Asian countries in particular, CJD cases are misdiagnosed and often underreported. Since Asia is the most populated continent in the world, the actual global prevalence of CJD cannot be estimated until and unless these countries are accounted for. Concrete and reliable surveillance networks are needed across Asia to evaluate the prevalence and incidence of CJD in the region. [Figure: see text]The graphical abstract demonstrates the prevalence of CJD cases in the world and systematically analyses the incidence of CJD in Asian countries between the year 1986-2022. Highest number of cases were reported in Japan followed by China. The study emphasizes the need for assimilation of Asian data in global prevalence.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10854368/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139698853","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}
Pub Date : 2024-12-01Epub Date: 2024-03-21DOI: 10.1080/19336896.2024.2329186
Andrea Bartolomé-Nafría, Javier García-Pardo, Salvador Ventura
Heterogeneous nuclear ribonucleoproteins (hnRNPs) are multifunctional proteins with integral roles in RNA metabolism and the regulation of alternative splicing. These proteins typically contain prion-like domains of low complexity (PrLDs or LCDs) that govern their assembly into either functional or pathological amyloid fibrils. To date, over 60 mutations targeting the LCDs of hnRNPs have been identified and associated with a spectrum of neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Alzheimer's disease (AD). The cryo-EM structures of pathological and functional fibrils formed by different hnRNPs have been recently elucidated, including those of hnRNPA1, hnRNPA2, hnRNPDL-2, TDP-43, and FUS. In this review, we discuss the structural features of these amyloid assemblies, placing particular emphasis on scrutinizing the impact of prevalent disease-associated mutations mapping within their LCDs. By performing systematic energy calculations, we reveal a prevailing trend of destabilizing effects induced by these mutations in the amyloid structure, challenging the traditionally assumed correlation between pathogenicity and amyloidogenic propensity. Understanding the molecular basis of this discrepancy might provide insights for developing targeted therapeutic strategies to combat hnRNP-associated diseases.
{"title":"Mutations in human prion-like domains: pathogenic but not always amyloidogenic.","authors":"Andrea Bartolomé-Nafría, Javier García-Pardo, Salvador Ventura","doi":"10.1080/19336896.2024.2329186","DOIUrl":"10.1080/19336896.2024.2329186","url":null,"abstract":"<p><p>Heterogeneous nuclear ribonucleoproteins (hnRNPs) are multifunctional proteins with integral roles in RNA metabolism and the regulation of alternative splicing. These proteins typically contain prion-like domains of low complexity (PrLDs or LCDs) that govern their assembly into either functional or pathological amyloid fibrils. To date, over 60 mutations targeting the LCDs of hnRNPs have been identified and associated with a spectrum of neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Alzheimer's disease (AD). The cryo-EM structures of pathological and functional fibrils formed by different hnRNPs have been recently elucidated, including those of hnRNPA1, hnRNPA2, hnRNPDL-2, TDP-43, and FUS. In this review, we discuss the structural features of these amyloid assemblies, placing particular emphasis on scrutinizing the impact of prevalent disease-associated mutations mapping within their LCDs. By performing systematic energy calculations, we reveal a prevailing trend of destabilizing effects induced by these mutations in the amyloid structure, challenging the traditionally assumed correlation between pathogenicity and amyloidogenic propensity. Understanding the molecular basis of this discrepancy might provide insights for developing targeted therapeutic strategies to combat hnRNP-associated diseases.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10962614/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140186323","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}
Pub Date : 2024-12-01Epub Date: 2024-05-12DOI: 10.1080/19336896.2024.2349017
Peter Hermann, Inga Zerr
Although the development of aggregation assays has noticeably improved the accuracy of the clinical diagnosis of prion diseases, research on biomarkers remains vital. The major challenges to overcome are non-invasive sampling and the exploration of new biomarkers that may predict the onset or reflect disease progression. This will become extremely important in the near future, when new therapeutics are clinically evaluated and eventually become available for treatment. This article aims to provide an overview of the achievements of biomarker research in human prion diseases, addresses unmet needs in the field, and points out future perspectives.
{"title":"Unmet needs of biochemical biomarkers for human prion diseases.","authors":"Peter Hermann, Inga Zerr","doi":"10.1080/19336896.2024.2349017","DOIUrl":"10.1080/19336896.2024.2349017","url":null,"abstract":"<p><p>Although the development of aggregation assays has noticeably improved the accuracy of the clinical diagnosis of prion diseases, research on biomarkers remains vital. The major challenges to overcome are non-invasive sampling and the exploration of new biomarkers that may predict the onset or reflect disease progression. This will become extremely important in the near future, when new therapeutics are clinically evaluated and eventually become available for treatment. This article aims to provide an overview of the achievements of biomarker research in human prion diseases, addresses unmet needs in the field, and points out future perspectives.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11093021/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140908967","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}
Pub Date : 2024-12-01Epub Date: 2024-04-26DOI: 10.1080/19336896.2024.2343298
Marc D Schwabenlander, Jason C Bartz, Michelle Carstensen, Alberto Fameli, Linda Glaser, Roxanne J Larsen, Manci Li, Rachel L Shoemaker, Gage Rowden, Suzanne Stone, W David Walter, Tiffany M Wolf, Peter A Larsen
Infectious prions are resistant to degradation and remain infectious in the environment for several years. Chronic wasting disease (CWD) has been detected in cervids inhabiting North America, the Nordic countries, and South Korea. CWD-prion spread is partially attributed to carcass transport and disposal. We employed a forensic approach to investigate an illegal carcass dump site connected with a CWD-positive herd. We integrated anatomic, genetic, and prion amplification methods to discover CWD-positive remains from six white-tailed deer (Odocoileus virginianus) and, using microsatellite markers, confirmed a portion originated from the CWD-infected herd. This approach provides a foundation for future studies of carcass prion transmission risk.
{"title":"Prion forensics: a multidisciplinary approach to investigate CWD at an illegal deer carcass disposal site.","authors":"Marc D Schwabenlander, Jason C Bartz, Michelle Carstensen, Alberto Fameli, Linda Glaser, Roxanne J Larsen, Manci Li, Rachel L Shoemaker, Gage Rowden, Suzanne Stone, W David Walter, Tiffany M Wolf, Peter A Larsen","doi":"10.1080/19336896.2024.2343298","DOIUrl":"https://doi.org/10.1080/19336896.2024.2343298","url":null,"abstract":"<p><p>Infectious prions are resistant to degradation and remain infectious in the environment for several years. Chronic wasting disease (CWD) has been detected in cervids inhabiting North America, the Nordic countries, and South Korea. CWD-prion spread is partially attributed to carcass transport and disposal. We employed a forensic approach to investigate an illegal carcass dump site connected with a CWD-positive herd. We integrated anatomic, genetic, and prion amplification methods to discover CWD-positive remains from six white-tailed deer (<i>Odocoileus virginianus</i>) and, using microsatellite markers, confirmed a portion originated from the CWD-infected herd. This approach provides a foundation for future studies of carcass prion transmission risk.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11057675/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140869098","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}
Pub Date : 2024-09-16DOI: 10.1080/19336896.2024.2402225
Anthony E Kincaid,Nathaniel D Denkers,Erin E McNulty,Caitlyn N Kraft,Jason C Bartz,Candace K Mathiason
Chronic wasting disease (CWD) is a transmissible and fatal prion disease that affects cervids. While both oral and nasal routes of exposure to prions cause disease, the spatial and temporal details of how prions enter the central nervous system (CNS) are unknown. Carotid bodies (CBs) are structures that are exposed to blood-borne prions and are densely innervated by nerves that are directly connected to brainstem nuclei, known to be early sites of prion neuroinvasion. All CBs examined contained mast cells expressing the prion protein which is consistent with these cells playing a role in neuroinvasion following prionemia.
{"title":"Expression of the cellular prion protein by mast cells in white-tailed deer carotid body, cervical lymph nodes and ganglia.","authors":"Anthony E Kincaid,Nathaniel D Denkers,Erin E McNulty,Caitlyn N Kraft,Jason C Bartz,Candace K Mathiason","doi":"10.1080/19336896.2024.2402225","DOIUrl":"https://doi.org/10.1080/19336896.2024.2402225","url":null,"abstract":"Chronic wasting disease (CWD) is a transmissible and fatal prion disease that affects cervids. While both oral and nasal routes of exposure to prions cause disease, the spatial and temporal details of how prions enter the central nervous system (CNS) are unknown. Carotid bodies (CBs) are structures that are exposed to blood-borne prions and are densely innervated by nerves that are directly connected to brainstem nuclei, known to be early sites of prion neuroinvasion. All CBs examined contained mast cells expressing the prion protein which is consistent with these cells playing a role in neuroinvasion following prionemia.","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142260258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-23DOI: 10.1080/19336896.2024.2343535
T. Outeiro, T. C. R. G. Vieira
ABSTRACT The history of human prion diseases began with the original description, by Hans Gerhard Creutzfeldt and by Alfons Maria Jakob, of patients with a severe brain disease that included speech abnormalities, confusion, and myoclonus, in a disease that was then named Creutzfeldt Jakob disease (CJD). Later, in Papua New Guinea, a disease characterized by trembling was identified, and given the name “Kuru”. Neuropathological examination of the brains from CJD and Kuru patients, and of brains of sheep with scrapie disease revealed significant similarities and suggested a possible common mode of infection that, at the time, was thought to derive from an unknown virus that caused slow infections. John Stanley Griffith hypothesized that the agent causing these diseases was “probably a protein without nucleic acid” and, in 1982, Stanley Prusiner reported the identification of a proteinaceous infectious particle (coining the term prion) that was resistant to inactivation methods that were at the time standard for nucleic acids, and identified PrP as the major protein component of the infectious agent in scrapie and in Creutzfeldt-Jakob disease, classifying this also as a prion disease. Interestingly, the prion concept had been previously expanded to yeast proteins capable of replicating their conformation, seeding their own aggregation and transmitting phenotypic information. The prion concept has been more recently expanded to refer to misfolded proteins that are capable of converting a normal form of a protein into an abnormal form. The quest to understand and treat prion diseases has united a specific research community around the topic, and regular meetings (Prion Meetings) have taken place over the years to enable discussions, train junior researchers, and inspire research in the field.
摘要 人类朊病毒疾病的历史始于汉斯-格哈德-克雅氏病(Hans Gerhard Creutzfeldt)和阿方斯-玛利亚-雅各布(Alfons Maria Jakob)对严重脑部疾病患者的最初描述,这些患者患有言语异常、精神错乱和肌阵挛等疾病,这种疾病当时被命名为克雅氏病(CJD)。后来,在巴布亚新几内亚发现了一种以颤抖为特征的疾病,并命名为 "库鲁"。对 CJD 和 Kuru 患者的大脑以及患有绵羊瘙痒症的绵羊大脑进行的神经病理学检查发现,这两种疾病具有显著的相似性,并表明可能存在一种共同的感染模式,当时人们认为这种模式源自一种可导致缓慢感染的未知病毒。约翰-斯坦利-格里菲斯(John Stanley Griffith)假设,导致这些疾病的病原体 "很可能是一种不含核酸的蛋白质"。1982 年,斯坦利-普鲁西纳(Stanley Prusiner)报告说,他发现了一种对当时核酸标准灭活方法具有抵抗力的蛋白型传染性颗粒(创造了朊病毒一词),并确定 PrP 为瘙痒病和克雅氏病中传染性病原体的主要蛋白质成分,将其也归类为朊病毒疾病。有趣的是,朊病毒的概念以前曾扩展到酵母蛋白质,它们能够复制自己的构象、播种自己的聚集体并传递表型信息。最近,朊病毒的概念被扩展为能够将正常形式的蛋白质转化为异常形式的错误折叠蛋白质。为了解和治疗朊病毒疾病,一个特定的研究团体围绕这一主题团结起来,多年来定期举行会议(朊病毒会议),以促进讨论、培训初级研究人员并激励该领域的研究。
{"title":"Prion meeting 2023: implications of a growing field","authors":"T. Outeiro, T. C. R. G. Vieira","doi":"10.1080/19336896.2024.2343535","DOIUrl":"https://doi.org/10.1080/19336896.2024.2343535","url":null,"abstract":"ABSTRACT The history of human prion diseases began with the original description, by Hans Gerhard Creutzfeldt and by Alfons Maria Jakob, of patients with a severe brain disease that included speech abnormalities, confusion, and myoclonus, in a disease that was then named Creutzfeldt Jakob disease (CJD). Later, in Papua New Guinea, a disease characterized by trembling was identified, and given the name “Kuru”. Neuropathological examination of the brains from CJD and Kuru patients, and of brains of sheep with scrapie disease revealed significant similarities and suggested a possible common mode of infection that, at the time, was thought to derive from an unknown virus that caused slow infections. John Stanley Griffith hypothesized that the agent causing these diseases was “probably a protein without nucleic acid” and, in 1982, Stanley Prusiner reported the identification of a proteinaceous infectious particle (coining the term prion) that was resistant to inactivation methods that were at the time standard for nucleic acids, and identified PrP as the major protein component of the infectious agent in scrapie and in Creutzfeldt-Jakob disease, classifying this also as a prion disease. Interestingly, the prion concept had been previously expanded to yeast proteins capable of replicating their conformation, seeding their own aggregation and transmitting phenotypic information. The prion concept has been more recently expanded to refer to misfolded proteins that are capable of converting a normal form of a protein into an abnormal form. The quest to understand and treat prion diseases has united a specific research community around the topic, and regular meetings (Prion Meetings) have taken place over the years to enable discussions, train junior researchers, and inspire research in the field.","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140668472","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-22DOI: 10.1080/19336896.2024.2343220
J. Mori, Nelda A Rivera, Jan Novakofski, N. Mateus-Pinilla
ABSTRACT Chronic wasting disease (CWD) is a fatal prion disease of the family Cervidae that circulates in both wild and captive cervid populations. This disease threatens the health and economic viability of the captive cervid industry, which raises cervids in contained spaces for purposes such as hunting and breeding. Given the high transmissibility and long incubation period of CWD, the introduction and propagation of the infectious prion protein within and between captive cervid farms could be devastating to individual facilities and to the industry as a whole. Despite this risk, there does not yet exist a literature review that summarizes the scientific knowledge, to date, about CWD spread, surveillance, or control measures. Our review, which focused on peer reviewed, primary research conducted in the United States, sought to address this need by searching Google Scholar, Scopus, and Web of Science with a five-term keyword string containing terms related to the (1) location, (2) species affected, (3) disease, (4) captive cervid industry, and (5) topic of focus. Between the three databases, there were 190 articles that were selected for further examination. Those articles were then read to determine if they were about CWD spread, surveillance, and/or control in captive cervid facilities. The 22 articles that met these inclusion criteria were evaluated in detail and discussed, with recommendations for future collaborative work between captive cervid owners, government agencies, and researchers. This work will help to address, inform, and mitigate the rising problem of CWD spread and establishment.
{"title":"A review of chronic wasting disease (CWD) spread, surveillance, and control in the United States captive cervid industry","authors":"J. Mori, Nelda A Rivera, Jan Novakofski, N. Mateus-Pinilla","doi":"10.1080/19336896.2024.2343220","DOIUrl":"https://doi.org/10.1080/19336896.2024.2343220","url":null,"abstract":"ABSTRACT Chronic wasting disease (CWD) is a fatal prion disease of the family Cervidae that circulates in both wild and captive cervid populations. This disease threatens the health and economic viability of the captive cervid industry, which raises cervids in contained spaces for purposes such as hunting and breeding. Given the high transmissibility and long incubation period of CWD, the introduction and propagation of the infectious prion protein within and between captive cervid farms could be devastating to individual facilities and to the industry as a whole. Despite this risk, there does not yet exist a literature review that summarizes the scientific knowledge, to date, about CWD spread, surveillance, or control measures. Our review, which focused on peer reviewed, primary research conducted in the United States, sought to address this need by searching Google Scholar, Scopus, and Web of Science with a five-term keyword string containing terms related to the (1) location, (2) species affected, (3) disease, (4) captive cervid industry, and (5) topic of focus. Between the three databases, there were 190 articles that were selected for further examination. Those articles were then read to determine if they were about CWD spread, surveillance, and/or control in captive cervid facilities. The 22 articles that met these inclusion criteria were evaluated in detail and discussed, with recommendations for future collaborative work between captive cervid owners, government agencies, and researchers. This work will help to address, inform, and mitigate the rising problem of CWD spread and establishment.","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140674328","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Prion disease is an infectious and fatal neurodegenerative disease. Western blotting (WB)-based identification of proteinase K (PK)-resistant prion protein (PrPres) is considered a definitive diagn...
朊病毒病是一种传染性致命神经退行性疾病。基于蛋白酶 K (PK) 抗性朊病毒蛋白 (PrPres) 的 Western 印迹 (WB) 鉴定被认为是一种明确的诊断方法。
{"title":"Novel method for classification of prion diseases by detecting PrPres signal patterns from formalin-fixed paraffin-embedded samples","authors":"Sachiko Koyama, Kaoru Yagita, Hideomi Hamasaki, Hideko Noguchi, Masahiro Shijo, Kosuke Matsuzono, Kei-Ichiro Takase, Keita Kai, Shin-Ichi Aishima, Kyoko Itoh, Toshiharu Ninomiya, Naokazu Sasagasako, Hiroyuki Honda","doi":"10.1080/19336896.2024.2337981","DOIUrl":"https://doi.org/10.1080/19336896.2024.2337981","url":null,"abstract":"Prion disease is an infectious and fatal neurodegenerative disease. Western blotting (WB)-based identification of proteinase K (PK)-resistant prion protein (PrPres) is considered a definitive diagn...","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":2.3,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140616697","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}