Prion and prion-like diseases in animals

Aguilar‐Calvo, Patricia; García, Consolación; Espinosa, Juan Carlos; Andréoletti, Olivier; Torres, Juan María

doi:10.1016/j.virusres.2014.11.026

Cited by 44 publications

(46 citation statements)

References 259 publications

(291 reference statements)

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“…Given the resilience of the infectious prion [23], the relative ease of transmission [24], and the uncertain interspecific barrier to transmission [25–27], a response plan is necessary as more is learned about the health and economic impacts of CWD. Therefore, management has primarily focused on containment utilizing various combinations of expanded surveillance, restrictions on movement or translocation of susceptible individuals, public hunting, and culling by government agencies [4,28–31].…”

Section: Introductionmentioning

confidence: 99%

Influence of the geographic distribution of prion protein gene sequence variation on patterns of chronic wasting disease spread in white-tailed deer (Odocoileus virginianus)

Brandt

Green

Ishida

et al. 2018

Prion

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Managing and controlling the spread of diseases in wild animal populations is challenging, especially for social and mobile species. Effective management benefits from information about disease susceptibility, allowing limited resources to be focused on areas or populations with a higher risk of infection. Chronic wasting disease (CWD), a transmissible spongiform encephalopathy that affects cervids, was detected in Colorado in the late 1960s. CWD was detected in Illinois and Wisconsin in 2002 and has since spread through many counties. Specific nucleotide variations in the prion protein gene (PRNP) sequence have been associated with reduced susceptibility to CWD in white-tailed deer. Though genetic resistance is incomplete, the frequency of deer possessing these mutations in a population is an important factor in disease spread (i.e. herd immunity). In this study we sequenced 625 bp of the PRNP gene from a sampling of 2433 deer from Illinois and Wisconsin. In north-central Illinois where CWD was first detected, counties had a low frequency of protective haplotypes (frequency <0.20); whereas in northwestern Illinois counties, where CWD cases have only more recently been detected, the frequency of protective haplotypes (frequency >0.30) was much higher (p < 0.05). Protective haplotype frequencies varied significantly among infected and uninfected geographic areas. The frequency of protective PRNP haplotypes may contribute to population level susceptibility and may shape the way CWD has spread through Illinois. Analysis of PRNP haplotype distribution could be a useful tool to assess CWD risk and allocate resources to contain and reduce the spread of infection.

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Section: Introductionmentioning

confidence: 99%

Influence of the geographic distribution of prion protein gene sequence variation on patterns of chronic wasting disease spread in white-tailed deer (Odocoileus virginianus)

Brandt

Green

Ishida

et al. 2018

Prion

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“…T ransmissible spongiform encephalopathies (TSEs), or prion diseases, are proteinaceous infectious neurodegenerative diseases affecting animals, including humans (3,4). The disease is caused by the accumulation of an aberrant misfolded form the presence of the normal cellular form of the prion protein, PrP C .…”

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confidence: 99%

Infectious Prions in the Pregnancy Microenvironment of Chronic Wasting Disease-Infected Reeves' Muntjac Deer

Nalls

McNulty

Hoover

et al. 2017

J Virol

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Ample evidence exists for the presence of infectious agents at the maternal-fetal interface, often with grave outcomes to the developing fetus (i.e., Zika virus, brucella, cytomegalovirus, and toxoplasma). While less studied, pregnancyrelated transmissible spongiform encephalopathies (TSEs) have been implicated in several species, including humans. Our previous work has shown that prions can be transferred from mother to offspring, resulting in the development of clinical TSE disease in offspring born to muntjac dams infected with chronic wasting disease (CWD) (1). We further demonstrated protein misfolding cyclic amplification (PMCA)-competent prions within the female reproductive tract and in fetal tissues harvested from CWD experimentally and naturally exposed cervids (1, 2). To assess whether the PMCA-competent prions residing at the maternal-fetal interface were infectious and to determine if the real-time quaking-induced conversion (RT-QuIC) methodology may enhance our ability to detect amyloid fibrils within the pregnancy microenvironment, we employed a mouse bioassay and RT-QuIC. In this study, we have demonstrated RT-QuIC seeding activity in uterus, placentome, ovary, and amniotic fluid but not in allantoic fluids harvested from CWD-infected Reeves' muntjac dams showing clinical signs of infection (clinically CWD-infected) and in some placentomes from pre-clinically CWD-infected dams. Prion infectivity was confirmed within the uterus, amniotic fluid, and the placentome, the semipermeable interface that sustains the developing fetus, of CWD-infected dams. This is the first report of prion infectivity within the cervid pregnancy microenvironment, revealing a source of fetal CWD exposure prior to the birthing process, maternal grooming, or encounters with contaminated environments.IMPORTANCE The facile dissemination of chronic wasting disease within captive and free-range cervid populations has led to questions regarding the transmission dynamics of this disease. Direct contact with infected animals and indirect contact with infectious prions in bodily fluids and contaminated environments are suspected to explain the majority of this transmission. A third mode of transmission, from mother to offspring, may be underappreciated. The presence of pregnancyrelated prion infectivity within the uterus, amniotic fluid, and the placental structure reveals that the developing fetus is exposed to a source of prions long before exposure to the infectious agent during and after the birthing process or via contact with contaminated environments. These findings have impact on our current concept of CWD disease transmission.KEYWORDS CWD, maternal, pregnancy, prions T ransmissible spongiform encephalopathies (TSEs), or prion diseases, are proteinaceous infectious neurodegenerative diseases affecting animals, including humans (3, 4). The disease is caused by the accumulation of an aberrant misfolded form

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“…Wildlife managers are concerned with transmissible spongiform encephalopathies (TSEs) as they are currently incurable, always fatal, and have the potential to cross species boundaries. Known TSEs include chronic wasting disease (CWD) in cervids, scrapie in sheep, bovine spongiform encephalopathy (BSE, also known as mad cow disease), transmissible mink encephalopathy (TME), feline spongiform encephalopathy (FSE) and Creutzfeld-Jacob in humans [1–3]. In response to health concerns of livestock and humans, research has focused on learning how species contract TSEs, how they are spread, causes of immunity, and prevention or cures [4].…”

Section: Introductionmentioning

confidence: 99%

Evolution of transmissible spongiform encephalopathy and the prion protein gene (PRNP) in mammals

Buchanan

Zink

2020

Preprint

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24Wildlife managers are concerned with transmissible spongiform encephalopathies (TSEs) as they 25 are currently incurable, always fatal, and have the potential to cross species boundaries. 26 Although a wide range of mammals exhibit TSEs, it is currently unclear whether they are 27 evolutionarily clustered or if TSE+ species are randomly distributed phylogenetically. We tested 28 whether mammalian species with TSEs are phylogenetically underdispersed on a tree derived 29 from 102 PRNP sequences obtained from the Orthologous Mammalian Markers database. We 30 determined that the PRNP tree was topologically congruent with a species tree for these same 31 102 taxa constructed from 20 aligned gene sequences, excluding the PRNP sequence. Searches 32 in Google Scholar were done to determine whether a species is known to have expressed a TSE. 33TSEs were present in a variety of orders excluding Chiroptera, Eulipotyphyla, and Lagomorpha 34 and no marine mammals (Artiodactyla) were recorded to have a TSE. We calculated the 35 phylogenetic signal of binary traits (D-Value) to infer if the phylogenetic distribution of TSEs 36 are conserved or dispersed. The occurrence of TSEs in both trees is non-random (Species tree 37 D-value = 0.291; PRNP tree D-value = 0.273), and appears to have arisen independently in the 38 recent history of different mammalian groups. Our findings suggest that the evolution of TSEs 39 develops in groups of species irrespective of PRNP genotype. The evolution of TSEs merits 40 continued exploration at a more in-depth phylogenetic level, as well as the search for genetic 41 combinations that might underlie TSE diseases.42 43 44 3 45 Introduction 46 Wildlife managers are concerned with transmissible spongiform encephalopathies (TSEs) 47 as they are currently incurable, always fatal, and have the potential to cross species boundaries. 48 Known TSEs include chronic wasting disease (CWD) in cervids, scrapie in sheep, bovine 49 spongiform encephalopathy (BSE, also known as mad cow disease), transmissible mink 50 encephalopathy (TME), feline spongiform encephalopathy (FSE) and Creutzfeld-Jacob in 51 humans [1-3]. In response to health concerns of livestock and humans, research has focused on 52 learning how species contract TSEs, how they are spread, causes of immunity, and prevention or 53 cures [4]. 54Most researchers accept the hypothesis that resistance to TSEs in mammals results from 55 certain genotypes found at the highly conserved prion protein gene (PRNP) [5] . TSEs are 56 thought to be caused by the misfolding of the host's prion protein (PrP) whose primary 57 physiological function is not entirely clear. When correctly folded the prion protein has been 58 theorized to localize at synaptic membranes and be related to normal synaptic functioning, signal 59 transduction, and copper binding [6][7][8][9]. When misfolded the protein induces other prion proteins 60 to misfold as well, followed by ultimately fatal accumulation in the central nervous system 61 within the host [1, 5, 10]. Misfolded ...

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Prion and prion-like diseases in animals

Cited by 44 publications

References 259 publications

Influence of the geographic distribution of prion protein gene sequence variation on patterns of chronic wasting disease spread in white-tailed deer (Odocoileus virginianus)

Influence of the geographic distribution of prion protein gene sequence variation on patterns of chronic wasting disease spread in white-tailed deer (Odocoileus virginianus)

Infectious Prions in the Pregnancy Microenvironment of Chronic Wasting Disease-Infected Reeves' Muntjac Deer

Evolution of transmissible spongiform encephalopathy and the prion protein gene (PRNP) in mammals

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