DOCSLIB.ORG

Prion Diseases an OVERVIEW for FUNERAL SERVICE PROFESSIONALS

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Prion Diseases an OVERVIEW for FUNERAL SERVICE PROFESSIONALS Prion Diseases AN OVERVIEW FOR FUNERAL SERVICE PROFESSIONALS BY MEGHAN LEWIS, KATIE GLISIC, DANIELLE JORDAN AND DR. BRIAN APPLEBY Mortuary professionals have encountered Disease, fatal familial insomnia and Gerstmann-Sträus- many potentially fatal and infectious diseases sler-Scheinker. and have successfully found ways to both Finally, the remaining cases are acquired through ei- ther ritualistic cannibalism (kuru), ingestion of prions serve families and protect the health of the from cattle infected with bovine spongiform encepha- community. Prion disease is no exception. lopathy (variant CJD, sometimes referred to as the hu- Prion diseases, also referred to as transmissible spongi- man equivalent to mad cow disease) or are secondary form encephalopathies (TSE), occur in humans and an- to receiving contaminated cadaver-derived growth hor- imals and primarily affect the central nervous system. mone, dura mater graft, corneal transplants or through The disease occurs when normal proteins spontaneously neurosurgical contamination. It is important to note that change to abnormal, disease-causing proteins. acquired prion diseases occur under very specific cir- There are three prion disease classifications: sporadic, cumstances. genetic and acquired. The majority are of sporadic etiolo- Prion disease is not transmissible from person to per- gy (85%) and include sporadic Creutzfeldt-Jakob Disease, son through normal contact or through environmental sporadic familial insomnia and variably protease-sensi- contamination. It is not spread through airborne drop- tive prionopathy. Genetic prion diseases account for 5% lets, as is tuberculosis, nor by blood, as are hepatitis and to 10% of cases and comprise familial Creutzfeldt-Jakob human immunodeficiency virus. The average worldwide occurrence of prion disease is CWD or other novel prion diseases can be transmitted roughly one to two cases per million people per year. to people. This number is consistent globally among countries Currently, the only way to confirm a diagnosis of pri- with surveillance centers. Despite being referred to as on disease is through autopsy and the examination and a “one in a million” disease (i.e., the incidence rate), the characterization of formalin-fixed and frozen brain tis- CDC estimates that approximately 1 out of every 6,000 sue. With funding from the CDC, NPDPSC offers a free- deaths in the United States is related to a prion disease of-charge brain-only autopsy to families with loved ones each year. This is due to the fact that age is a risk fac- suffering from suspected prion disease. At this time, the tor for developing the disease and of the variation of ill- center is not aware of any state that requires an autop- ness duration. Given this number, it is highly likely that sy in cases of suspected prion disease/CJD. Enrollment a mortuary professional has served a family whose loved in the program is voluntary and can be withdrawn at one died from a diagnosed or even undiagnosed prion any time prior to autopsy. Families often choose to en- disease. Within the scientific community, prion disease roll their loved one in the program so they can confirm a is known as the perfect “mimicker” of other well-known diagnosis, determine the subtype and learn whether the neurodegenerative diseases, including Alzheimer’s, Par- disease is sporadic or genetic in etiology. The center cov- kinson’s, Lewy Body Dementia, etc., due to the overlap ers all autopsy-related expenses, including but not limit- of symptoms. ed to round-trip transportation between the storage and Prion disease is a rapidly progressive neurodegener- autopsy site (as needed), testing for prion disease and ad- ative disorder. There is currently no cure or treatment, ditional miscellaneous costs. and it is, unfortunately, always fatal. The majority of pa- The center’s network of public and private autopsy pro- tients die within one year of disease onset, with a mean viders across the country works closely with mortuary duration of four to six months. Treatment focuses on professionals to make arrangements and provide educa- minimizing symptoms and maintaining quality of life tion regarding the disease. It is the responsibility of the for both patients and their family/caregivers. contracted mortuary professional to remove a decedent Once a diagnosis of prion disease is made, it is recom- from their place of death. For patients enrolled into our mended that end-of-life concerns be addressed quickly. autopsy program, the center requests that the body is re- Hospice care is usually brought in, and it is recommend- frigerated within four hours of death or as soon as pos- ed that families make pre-arrangements with a funeral sible. A body can be safely and discreetly removed using home, including whether the family wishes for a post- appropriate standard infection control measures, includ- mortem examination before cremation/embalming. ing personal protective equipment. No special precau- tions are required. The National Prion Disease Pathology Surveillance Cen- Patients enrolled in the center’s autopsy program are ter (NPDPSC) was established in 1997 in the Department cared for with dignity. Its staff and licensed mortician of Pathology at Case Western Reserve University. Its pur- take painstaking care to ensure that the level of trans- pose is to acquire tissue samples and clinical information missibility of prion disease is at a minimum. from as many cases of human prion disease occurring in the United States as possible in order to help monitor the Misinformation circulated regarding prion disease can possible occurrence of variant CJD and other emerging be a considerable barrier affecting the care and compas- prion diseases in the country. It also assists clinicians in sion that is extended to families. Education is difficult making a clinical diagnosis of prion disease by offering for numerous reasons. Given that prion disease is rare, it a variety of tests, including cerebrospinal fluid and ge- is not a disease with which many mortuary profession- netic testing. als are familiar. Misinformation about how to handle Although the United States has seen only a few cas- the decedent and the transmissibility of the disease has es of bovine spongiform encephalopathy in our cattle often resulted in families being denied services such as herds, chronic wasting disease (CWD), a prion disease embalming. Per the CDC, embalming bodies of CJD pa- of elk and deer in both free range and captive herds, has tients who have been autopsied can be safely performed been spreading across North America over the past few using standard infection control measures as outlined decades. Since there are an estimated 22 million elk and in the protocol “Infection Control Guidelines for Trans- deer in the United States and a large number of hunters missible Spongiform Encephalopathies,” distributed by who consume elk and deer meat, many humans could be the World Health Organization (WHO). An open-casket potentially exposed to CWD. To date, there have been no viewing should not be prohibited. However, if an autop- reported cases of CWD infection in humans. sy has been performed, it is recommended that family The NPDPSC coordinates with the Centers for Disease members be advised to avoid superficial contact with the Control and Prevention, as well as with individual state body (such as touching or kissing the decedent’s face). health departments to monitor cases from CWD-endem- There are also no special burial or cremation require- ic areas. Furthermore, it is doing experimental research ments. Interment of bodies in closed caskets presents no on CWD transmissibility using animal models. Con- significant environmental contamination risk, and cre- tinued surveillance is necessary to investigate whether mated remains can be considered sterile and safe as the www.nfda.org June 2019 51 To increase your knowledge about prion LEARN diseases, also check out these resources: has partnered with CJDF to provide education and sup- MORE • cdc.gov/prions/cjd/funeral-directors.html port to mortuary professionals regarding servicing fam- • cjdsurveillance.com ilies with suspected prion disease. Our autopsy team, • cjdfoundation.org along with our licensed funeral director and mortician, has participated in continuing education seminars for the Embalmers Association of Cleveland, the Alabama infection agent does not survive cremation temperatures. Funeral Directors Association, the Funeral Directors As- According to the aforementioned WHO guidelines, any sociation of the Falls Cities and the annual conference of mortuary working surfaces that accidentally become the Oregon Funeral Directors Association. contaminated with a potential CJD agent (e.g., spinal flu- It is our goal that through our various outreach ef- id, brain tissue, etc.) should be flooded with sodium hy- forts and continuing education seminars, we can assist droxide or bleach, left undisturbed for at least one hour, and educate funeral and mortuary professionals in the then (using gloves) mopped up with absorbent dispos- appropriate handling of prion disease patients. We also able rags and surfaces swabbed with sufficient water to aim to clear up any misconceptions or misinformation remove any residual disinfectant solution. The NPDPSC about the disease that may be prohibiting the use of a fa- serves as a resource for funeral homes and embalmers; cility due to a prion disease diagnosis and the family’s its autopsy team is available to answer any questions and wishes of an
Load more

Recommended publications
  • Montana Fish, Wildlife & Parks' 2020 Chronic Wasting Disease
    Montana Fish, Wildlife & Parks’ 2020 Chronic Wasting Disease Surveillance and Monitoring Report Federal Aid in Wildlife Restoration Grant W-171-M Annual report, May 14, 2021 Dr. Emily Almberg Matthew Becker Disease Ecologist, MTFWP Wildlife Veterinary Technician, MTFWP 1400 S. 19th Avenue, Bozeman, MT 59718 1400 S. 19th Avenue, Bozeman, MT 59718 406-577-7881, [email protected] 406-577-7882, [email protected] Justin Gude John Thornburg Wildlife Research & Technical Services CWD Program Lead Technician, MTFWP Bureau Chief, MTFWP 1400 S. 19th Avenue, Bozeman, MT 59718 1420 E. 6th Avenue, Helena, MT 59620 406-577-7883, [email protected] 406-444-3767, [email protected] Dr. Jennifer Ramsey Wildlife Veterinarian, MTFWP 1400 S. 19th Avenue, Bozeman, MT 59718 406-577-7880, [email protected] STATE: Montana AGENCY: Fish, Wildlife & Parks GRANT: Montana Wildlife Disease Surveillance & Response Program MT TRACKING: W-171-M Executive Summary Montana Fish, Wildlife, and Parks (FWP) has been conducting surveillance for chronic wasting disease (CWD) since 1998, and first detected CWD in wild deer in 2017. In 2020, FWP prioritized sampling in northwestern, southwestern, and eastern/southeastern Montana. In addition, FWP continued to target sampling in the Libby CWD Management Zone and organized a special CWD hunt known as the Southwestern Montana CWD Management Hunt. FWP offered free state-wide testing available via mail-in, CWD-check stations, and all regional FWP headquarter offices in 2020. During the 2020 season, FWP tested 7974 samples from mule deer (n=3108), white-tailed deer (n=4088), elk (n=729), and moose (n=49). Of these, 271 animals tested positive for CWD, including 38 mule deer and 233 white-tailed deer.
    [Show full text]
  • Vaccination with Prion Peptide-Displaying Polyomavirus-Like Particles Prolongs Incubation Time in Scrapie-Infected Mice
    viruses Article Vaccination with Prion Peptide-Displaying Polyomavirus-Like Particles Prolongs Incubation Time in Scrapie-Infected Mice Martin Eiden 1,* , Alma Gedvilaite 2 , Fabienne Leidel 1,3, Rainer G. Ulrich 1 and Martin H. Groschup 1 1 Institute of Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Südufer 10, 17493 Greifswald-Insel Riems, Germany; [email protected] (F.L.); rainer.ulrich@fli.de (R.G.U.); martin.groschup@fli.de (M.H.G.) 2 Life Sciences Center, Institute of Biotechnology, Vilnius University, Sauletekio˙ al. 7, LT-10257 Vilnius, Lithuania; [email protected] 3 Task Force Animal Diseases, Darmstadt Regional Administrative Council, Luisenplatz 2, 64283 Darmstadt, Germany * Correspondence: martin.eiden@fli.de Abstract: Prion diseases like scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle or Creutzfeldt–Jakob disease (CJD) in humans are fatal neurodegenerative diseases characterized by the conformational conversion of the normal, mainly α-helical cellular prion protein (PrPC) into the abnormal β-sheet rich infectious isoform PrPSc. Various therapeutic or prophylactic approaches have been conducted, but no approved therapeutic treatment is available so far. Immunisation against prions is hampered by the self-tolerance to PrPC in mammalian species. One strategy to avoid this tolerance is presenting PrP variants in virus-like particles (VLPs). Therefore, we vaccinated C57/BL6 mice with nine prion peptide variants presented by hamster polyomavirus capsid protein VP1/VP2-derived VLPs. Mice were subsequently challenged intraperitoneally with the murine RML Citation: Eiden, M.; Gedvilaite, A.; prion strain. Importantly, one group exhibited significantly increased mean survival time of 240 days Leidel, F.; Ulrich, R.G.; Groschup, M.H.
    [Show full text]
  • Zinc and Copper Ions Differentially Regulate Prion-Like Phase
    viruses Article Zinc and Copper Ions Differentially Regulate Prion-Like Phase Separation Dynamics of Pan-Virus Nucleocapsid Biomolecular Condensates Anne Monette 1,* and Andrew J. Mouland 1,2,* 1 Lady Davis Institute at the Jewish General Hospital, Montréal, QC H3T 1E2, Canada 2 Department of Medicine, McGill University, Montréal, QC H4A 3J1, Canada * Correspondence: [email protected] (A.M.); [email protected] (A.J.M.) Received: 2 September 2020; Accepted: 12 October 2020; Published: 18 October 2020 Abstract: Liquid-liquid phase separation (LLPS) is a rapidly growing research focus due to numerous demonstrations that many cellular proteins phase-separate to form biomolecular condensates (BMCs) that nucleate membraneless organelles (MLOs). A growing repertoire of mechanisms supporting BMC formation, composition, dynamics, and functions are becoming elucidated. BMCs are now appreciated as required for several steps of gene regulation, while their deregulation promotes pathological aggregates, such as stress granules (SGs) and insoluble irreversible plaques that are hallmarks of neurodegenerative diseases. Treatment of BMC-related diseases will greatly benefit from identification of therapeutics preventing pathological aggregates while sparing BMCs required for cellular functions. Numerous viruses that block SG assembly also utilize or engineer BMCs for their replication. While BMC formation first depends on prion-like disordered protein domains (PrLDs), metal ion-controlled RNA-binding domains (RBDs) also orchestrate their formation. Virus replication and viral genomic RNA (vRNA) packaging dynamics involving nucleocapsid (NC) proteins and their orthologs rely on Zinc (Zn) availability, while virus morphology and infectivity are negatively influenced by excess Copper (Cu). While virus infections modify physiological metal homeostasis towards an increased copper to zinc ratio (Cu/Zn), how and why they do this remains elusive.
    [Show full text]
  • Chronic Wasting Disease and Atypical Forms of Bovine Spongiform
    Journal of General Virology (2012), 93, 1624–1629 DOI 10.1099/vir.0.042507-0 Short Chronic wasting disease and atypical forms of Communication bovine spongiform encephalopathy and scrapie are not transmissible to mice expressing wild-type levels of human prion protein Rona Wilson,1 Chris Plinston,1 Nora Hunter,1 Cristina Casalone,2 Cristiano Corona,2 Fabrizio Tagliavini,3 Silvia Suardi,3 Margherita Ruggerone,3 Fabio Moda,3 Silvia Graziano,4 Marco Sbriccoli,4 Franco Cardone,4 Maurizio Pocchiari,4 Loredana Ingrosso,4 Thierry Baron,5 Juergen Richt,63 Olivier Andreoletti,7 Marion Simmons,8 Richard Lockey,8 Jean C. Manson1 and Rona M. Barron1 Correspondence 1Neuropathogenesis Division, The Roslin Institute and R(D)SVS, University of Edinburgh, Roslin, Rona M. Barron Midlothian, UK [email protected] 2Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle d’Aosta, Turin, Italy 3IRCCS Foundation, ‘Carlo Besta’ Neurological Institute, Milan, Italy 4Department of Cell Biology and Neurosciences, Istituto Superiore di Sanita`, Viale Regina Elena 299, 00161 Rome, Italy 5Agence Nationale de Se´curite´ Sanitaire, Lyon, France 6USDA, ARS, National Animal Disease Center, PO Box 70, Ames, IA 50010, USA 7UMR 1225 Interactions Hoˆtes-Agents Pathoge`nes, INRA, Ecole Nationale Ve´te´rinaire, 23 chemin des Capelles, B.P. 87614, 31076 Toulouse Cedex 3, France 8Neuropathology Section, Department of Pathology and Host Susceptibility, Animal Health and Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, UK The association between bovine spongiform encephalopathy (BSE) and variant Creutzfeldt–Jakob disease (vCJD) has demonstrated that cattle transmissible spongiform encephalopathies (TSEs) can pose a risk to human health and raises the possibility that other ruminant TSEs may be transmissible to humans.
    [Show full text]
  • Prion Diseases in Knock-In Mice Carrying Single Prp Codon Substitutions Associated with Human Diseases
    Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases Walker S. Jacksona,b,c,1, Andrew W. Borkowskia,b,c, Nicki E. Watsona, Oliver D. Kingd, Henryk Faase, Alan Jasanoffe,f, and Susan Lindquista,b,c,2 aWhitehead Institute for Biomedical Research, Cambridge, MA 02142; bHoward Hughes Medical Institute, cDepartment of Biology, and fDepartments of Biological Engineering, Brain and Cognitive Sciences, and Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139; dDepartment of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, MA 01655; and eFrances Bitter Magnet Laboratory, Cambridge, MA 02139 Contributed by Susan Lindquist, July 9, 2013 (sent for review March 7, 2013) In man, mutations in different regions of the prion protein (PrP) linked to it, provides an important general model for such are associated with infectious neurodegenerative diseases that investigations. have remarkably different clinical signs and neuropathological There are several types of human prion diseases, each begin- lesions. To explore the roots of this phenomenon, we created ning with pathologic processes in a different brain region and fi – a knock-in mouse model carrying the mutation associated with leading to distinct functional de cits: cognition [Creutzfeldt – – one of these diseases [Creutzfeldt–Jakob disease (CJD)] that was Jakob disease (CJD)], movement control (Gerstmann Sträussler Scheinker syndrome), or sleep and autonomic functions [fatal exactly analogous to a previous knock-in model of a different fl prion disease [fatal familial insomnia (FFI)]. Together with the familial insomnia (FFI)] (7). Prion diseases also af ict animals WT parent, this created an allelic series of three lines, each express- and include bovine spongiform encephalopathy (BSE) of cattle, scrapie of sheep and goats, and chronic wasting disease (CWD) ing the same protein with a single amino acid difference, and with of deer and elk (1).
    [Show full text]
  • Mitochondrial Dysfunction in Preclinical Genetic Prion Disease: a Target for 7 Preventive Treatment?
    1HXURELRORJ\RI'LVHDVH ² Contents lists available at ScienceDirect Neurobiology of Disease journal homepage: www.elsevier.com/locate/ynbdi Mitochondrial dysfunction in preclinical genetic prion disease: A target for 7 preventive treatment? Guy Kellera,c,1, Orli Binyamina,c,1, Kati Frida,c, Ann Saadab,c, Ruth Gabizona,c,⁎ a Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Israel b Department of Genetics and Metabolic Diseases, The Monique and Jacques Roboh Department of Genetic Research, Hadassah-Hebrew University Medical Center, Israel c Medical School, The Hebrew University, Jerusalem, Israel ABSTRACT Mitochondrial malfunction is a common feature in advanced stages of neurodegenerative conditions, as is the case for the accumulation of aberrantly folded proteins, such as PrP in prion diseases. In this work, we investigated mitochondrial activity and expression of related factors vis a vis PrP accumulation at the subclinical stages of TgMHu2ME199K mice, modeling for genetic prion diseases. While these mice remain healthy until 5–6 months of age, they succumb to fatal disease at 12–14 months. We found that mitochondrial respiratory chain enzymatic activates and ATP/ROS production, were abnormally elevated in asymptomatic mice, concomitant with initial accumulation of disease related PrP. In parallel, the expression of Cytochrome c oxidase (COX) subunit IV isoform 1(Cox IV-1) was reduced and replaced by the activity of Cox IV isoform 2, which operates in oxidative neuronal conditions. At all stages of disease, Cox IV-1 was absent from cells accu- mulating disease related PrP, suggesting that PrP aggregates may directly compromise normal mitochondrial function. Administration of Nano-PSO, a brain targeted antioxidant, to TgMHu2ME199K mice, reversed functional and biochemical mitochondrial functions to normal conditions regardless of the presence of misfolded PrP.
    [Show full text]
  • An Evolutionary Basis for Scrapie Disease : Identification of a Fish
    72 Update TRENDS in Genetics Vol.19 No.2 February 2003 affect regulation of the human genome in a more global 11 Frith, M.C. et al. (2002) Statistical significance of clusters of motifs manner by creating S/MARs that form chromatin loops, represented by position specific scoring matrices in nucleotide and by shaping the sequence evolution of LCRs. sequences. Nucleic Acids Res. 30, 3214–3224 12 Wingender, E. et al. (2001) The TRANSFAC system on gene expression regulation. Nucleic Acids Res. 29, 281–283 Acknowledgements 13 Purucker, M. et al. (1990) Structure and function of the enhancer 30 to Galina V. Glazko was supported by research grants from NIH (GM-20293) the human A gamma globin gene. Nucleic Acids Res. 18, 7407–7415 and NASA (NCC2-1057) awarded to Masatoshi Nei. We thank Nathan 14 Li, Q. et al. (1999) Locus control regions: coming of age at a decade plus. J. Bowen and Wolfgang J. Miller for discussions on the relationship Trends Genet. 15, 403–408 between TEs and S/MARs. 15 Hardison, R. et al. (1997) Locus control regions of mammalian beta- globin gene clusters: combining phylogenetic analyses and exper- References imental results to gain functional insights. Gene 205, 73–94 1 The Human Genome Sequencing Consortium, (2001) Initial sequen- 16 Strausberg, R. et al. (1999) The mammalian gene collection. Science cing and analysis of the human genome. Nature 409, 860–921 286, 455–457 2 Kidwell, M.G. and Lisch, D.R. (2001) Perspective: transposable 17 Bode, J. et al. (1996) Scaffold/matrix-attached regions: topological elements, parasitic DNA, and genome evolution.
    [Show full text]
  • Chronic Wasting Disease
    COLORADO PARKS & WILDLIFE Chronic Wasting Disease RECENT TRENDS & IMPLICATIONS IN COLORADO Maintaining wildlife health is a fundamental component of sound wildlife management and is regarded as a high priority in Colorado. Colorado Parks and Wildlife is dedicated to delivering a coordinated and systematic approach for monitoring, investigating, reporting, and – where feasible – controlling health problems in free- ranging wildlife. hronic wasting disease (CWD) is well- established in deer, elk, and moose herds throughout Cmuch of Colorado. As of January 2018, 31 of 55 deer data analysis units (DAUs), 14 of 43 elk DAUs, and 2 of 9 moose DAUs have become infected. This prion disease also has been reported in deer, elk, moose, and reindeer (caribou) in 27 other states and provinces, in South Korea, and most recently in Norway. The rate of CWD infection (or “prevalence”) appears to be rising in many affected Colorado herds. However, trends have become difficult to track in the last 10 years because too few hunters voluntarily submit samples for testing. As a result, our current prevalence estimates for many herds are imprecise and perhaps somewhat biased. In 2017, CPW resumed mandatory harvest submissions in select DAUs. Sample sizes in the targeted DAUs increased 10-fold, yielding better data to inform herd management planning. Reliable CWD prevalence estimates and trend assessments are needed to inform deer and elk conservation in Colorado. Figure. Chronic wasting disease harvest and prevalence A growing body of data suggests that unchecked CWD trends in three Colorado mule deer DAUs illustrate patterns epidemics impair the long-term performance of affected and potential relationships between harvest and disease populations.
    [Show full text]
  • NYS Interagency CWD Risk Minimization Plan
    New York State Interagency CWD Risk Minimization Plan New York State Department of Environmental Conservation Division of Fish and Wildlife Division of Law Enforcement New York State Department of Agriculture and Markets Division of Animal Industry Cornell University College of Veterinary Medicine Animal Health Diagnostic Center Prepared February 2018 Taking an ecosystem approach also means recognizing the North American deer herds as one and not two entities. While some cooperation exists between regulators of wildlife and livestock, it is clearly insufficient and almost non-existent in some jurisdictions. That cooperation also needs to include both game farmers and hunters, who have the most to lose in the long term. The time for finger pointing is over; the time for an integrated approach has begun. – P. James 2008 Both Sides of the Fence: A Strategic Review of Chronic Wasting Disease 1 | N Y S C W D R i s k M i n i m i z a t i o n P l a n Executive Summary Chronic wasting disease (CWD) represents a serious threat to New York State’s wild white-tailed deer and moose populations and captive cervid industry with potentially devastating economic, ecological, and social repercussions. This plan presents recommendations to reasonably minimize the risk of re- entry and spread of chronic wasting disease (CWD) in New York State from an Interagency CWD Team, comprised of New York State Department of Environmental Conservation (DEC) Division of Fish and Wildlife, DEC Division of Law Enforcement, New York State Department of Agriculture and Markets (DAM) Division of Animal Industry, and Cornell University College of Veterinary Medicine Wildlife Health faculty.
    [Show full text]
  • Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion
    Article DOI: https://doi.org/10.3201/eid2309.161474 Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion Technical Appendix Additional Data Brain homogenates from all mice (experimentally infected animals and uninfected controls) were analyzed for the presence of PrP-res. Proteinase K-resistant PrP was detected in all mice infected with H95+ prions (Figure 1) demonstrating that H95+ is 100% penetrant. PrP- res was not, however, detected in mice infected with the Wisc-1 strain from wt/wt or S96/wt deer or CWD2 from elk. A similar analysis of brain homogenates from hamsters was also performed. Wisc-1 CWD was preferentially transmitted to hamsters upon primary passage (Figure 2). Wt/wt CWD caused clinical disease or subclinical accumulation of PrP-res in exposed hamsters. Transmission of S96/wt and H95/wt CWD prions resulted, primarily, in subclinical disease. Inoculation of elk CWD prions resulted in clinical disease in two out of five hamsters and subclinical disease in one animal. The H95/S96 isolate transmitted inefficiently with only one of eight hamsters having subclinical disease. This subclinical infection may be due to Wisc-1 in the H95/S96 deer isolate. Hamsters inoculated with uninfected deer brain homogenate did not show signs of prion disease nor accumulate PrP-res. Secondary structure of host PrP influences the ability of a strain to propagate in a new host. Based on NMR studies, it has been hypothesized that amino acid variation at residues 170- 175 (Figure 3) in PrPC results in a loop structure between beta-sheet 2 and alpha-helix 2 (β2-α2) whose flexibility influences the outcome of interspecies transmissions (1–7).
    [Show full text]
  • Prion Disease Reporting and Investigation Guideline
    Human Prion Diseases Transmissible spongiform encephalopathies (TSE) including Creutzfeldt - Jakob disease (CJD) Illness The causative agent is thought to be a misfolded infectious isoform, called PrPSc, of a normally occurring cellular protein, PrPC. The abnormal folding can occur spontaneously (sporadic), by genetic mutations (familial), or by the uptake of prions from an external source (iatrogenic, variant). Accumulation of PrPSc in the central nervous system causes progressive neurodegenerative spongiform changes. An average of 12 cases occur in Washington annually. No cases of variant CJD have been reported in Washington state to date. Signs and In sporadic cases: rapidly progressive dementia, visual disturbances, cerebellar dysfunction, Symptoms pyramidal and extra pyramidal dysfunction, and myoclonus. In variant cases: behavioral changes (psychosis, depression), painful sensory symptoms, and delayed neurologic signs. See Appendix A Incubation Variable, but very long; in the order of years to decades. Case Please see https://www.cdc.gov/prions/cjd/diagnostic-criteria.html for sporadic, familial, and Classification iatrogenic CJD and https://www.cdc.gov/prions/vcjd/diagnostic-criteria.html for variant CJD. Report all definite, probable and possible cases to CDE Differential Alzheimer’s disease, dementia with Lewy bodies, frontotemporal dementia, corticobasal diagnosis degeneration, progressive supranuclear palsy, neoplasms, viral encephalitis, metal toxicity Treatment Always fatal; death usually occurs within a year after onset of illness. Treatment is supportive. Laboratory/ Confirmatory testing requires pathologic examination of brain tissue. Pathologic and CSF testing Imaging are performed only at the National Prion Disease Pathology Surveillance Center (NPDPSC). See NPDPSC website for collection and shipment details. Tests for prion diseases are not performed at Public Health Laboratories (PHL).
    [Show full text]
  • Lecture 1: INTRODUCTION in MEDICAL BIOLOGY. CELL STRUCTURE
    Lecture 1: INTRODUCTION IN MEDICAL BIOLOGY. CELL STRUCTURE 1. Biology: The Science of Our Lives 2. Theories Contributing to Modern Biology: Cell Theory 3. Forms and Diversity of Life 4. Levels of Organization 5. Cell Structure Biology (from Greek βίος - life and λόγος - word, judgement) – is a branch of the natural sciences, and is the study of living organisms and their interactions with environment. The term was specially proposed by French naturalist Jean-Baptiste Pierre Antoine de Monet, Chevalier de Lamarck in 1802 Biology deals with every aspect of life in a living organism. Biology examines the structure, function, growth, origin, evolution, and distribution of living things. Modern biology is complex of sciences. Most biological sciences are specialized disciplines: Botany, Zoology, Protozoology, Microbiology, Virology, Molecular biology, Genetics, Embryology, Evolution theory, Ecology and so on. The history of biology traces the study of the living world from ancient to modern times. Although the concept of biology as a single coherent field arose in the 19th century, the biological sciences emerged from traditions of medicine and natural history reaching back to ancient Egyptian medicine and the works of Aristotle and Galen in the ancient Greco-Roman world, which were then further developed in the Middle Ages by Muslim physicians and scholars such as al-Jahiz, Avicenna, Avenzoar, Ibn al-Baitar and Ibn al-Nafis. Ancient Greek philosopher, Aristotle developed his Scala Naturae, or Ladder of Life, to explain his concept of the advancement
    [Show full text]