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At least 37 records · Page 2Linked to original sources
USGS2011

Degradation of the disease-associated prion protein by a serine protease from lichens

The disease-associated prion protein (PrP(TSE)), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, are ubiquitous in the environment and have evolved unique biological activities allowing their survival in challenging ecological niches. We investigated PrP(TSE) inactivation by lichens and found acetone extracts of three lichen species (Parmelia sulcata, Cladonia rangiferina and Lobaria pulmonaria) have the ability to degrade prion protein (PrP) from TSE-infected hamsters, mice and deer. Immunoblots measuring PrP levels and protein misfolding cyclic amplification indicated at least two logs of reductions in PrP(TSE). Degradative activity was not found in closely related lichen species or in algae or a cyanobacterium that inhabit lichens. Degradation was blocked by Pefabloc SC, a serine protease inhibitor, but not inhibitors of other proteases or enzymes. Additionally, we found that PrP levels in PrP(TSE)-enriched preps or infected brain homogenates are also reduced following exposure to freshly-collected P. sulcata or an aqueous extract of the lichen. Our findings indicate that these lichen extracts efficiently degrade PrP(TSE) and suggest that some lichens could have potential to inactivate TSE infectivity on the landscape or be a source for agents to degrade prions. Further work to clone and characterize the protease, assess its effect on TSE infectivity and determine which organism or organisms present in lichens produce or influence the protease activity is warranted.

PLoS ONE↗
USGS2014

Humic substances interfere with detection of pathogenic prion protein

Studies examining the persistence of prions (the etiological agent of transmissible spongiform encephalopathies) in soil require accurate quantification of pathogenic prion protein (PrP TSE ) extracted from or in the presence of soil particles. Here, we demonstrate that natural organic matter (NOM) in soil impacts PrP TSE detection by immunoblotting. Methods commonly used to extract PrPTSE from soils release substantial amounts of NOM, and NOM inhibited PrPTSE immunoblot signal. The degree of immunoblot interference increased with increasing NOM concentration and decreasing NOM polarity. Humic substances affected immunoblot detection of prion protein from both deer and hamsters. We also establish that after interaction with humic acid, PrP TSE remains infectious to hamsters inoculated intracerebrally, and humic acid appeared to slow disease progression. These results provide evidence for interactions between PrPTSE and humic substances that influence both accurate measurement of PrP TSE in soil and disease transmission.

Soil Biology and Biochemistry↗
USGS2017

CWDPRNP: A tool for cervid prion sequence analysis in program R

Chronic wasting disease is a fatal, neurological disease caused by an infectious prion protein, which affects economically and ecologically important members of the family Cervidae. Single nucleotide polymorphisms within the prion protein gene have been linked to differential susceptibility to the disease in many species. Wildlife managers are seeking to determine the frequencies of disease-associated alleles and genotypes and delineate spatial genetic patterns. The CWDPRNP package, implemented in program R, provides a unified framework for analyzing prion protein gene variability and spatial structure.

Bioinformatics↗
USGS2011

Degradation of the disease-associated prion protein by a serine protease from lichens.

The disease-associated prion protein (PrP TSE ), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, are ubiquitous in the environment and have evolved unique biological activities allowing their survival in challenging ecological niches. We investigated PrP TSE inactivation by lichens and found acetone extracts of three lichen species ( Parmelia sulcata , Cladonia rangiferina and Lobaria pulmonaria ) have the ability to degrade prion protein (PrP) from TSE-infected hamsters, mice and deer. Immunoblots measuring PrP levels and protein misfolding cyclic amplification indicated at least two logs of reductions in PrP TSE . Degradative activity was not found in closely related lichen species or in algae or a cyanobacterium that inhabit lichens. Degradation was blocked by Pefabloc SC, a serine protease inhibitor, but not inhibitors of other proteases or enzymes. Additionally, we found that PrP levels in PrP TSE -enriched preps or infected brain homogenates are also reduced following exposure to freshly-collected P. sulcata or an aqueous extract of the lichen. Our findings indicate that these lichen extracts efficiently degrade PrP TSE and suggest that some lichens could have potential to inactivate TSE infectivity on the landscape or be a source for agents to degrade prions. Further work to clone and characterize the protease, assess its effect on TSE infectivity and determine which organism or organisms present in lichens produce or influence the protease activity is warranted.

Michigan, Minnesota, Oregon, Wisconsin↗
USGS2025

Prion gene sequencing in Florida panthers (Puma concolor coryi) suggests no differential susceptibility to transmissible spongiform encephalopathy

Transmissible spongiform encephalopathy, or prion disease, poses a serious threat to wildlife; however, the susceptibility of apex predators is still being assessed. We investigated variation in the prion protein gene in Florida panthers ( Puma concolor coryi ) and found that admixture from Central American pumas probably introduced a novel, albeit benign, prion allele.

Journal of Wildlife Diseases↗
USGS2019

Spatial heterogeneity of prion gene polymorphisms in an area recently infected by chronic wasting disease

Genetic variability in the prion protein ( Prnp ) gene influences host susceptibility to many pathogenic prion diseases. Understanding the distribution of susceptible Prnp variants and determining factors influencing spatial genetic patterns are important components of many chronic wasting disease mitigation strategies. Here, we describe Prnp variability in white-tailed deer ( Odocoileus virginianus ) from the Mid-Atlantic region of the United States of America, an area with a recent history of infection and low disease incidence. This population is characterized by lower rates of polymorphism and significantly higher frequencies of the more susceptible 96GG genotype compared to previously surveyed populations. The prevalence of the most susceptible genotypes at disease-associated loci did vary among subregions, indicating that populations have innate differences in genotype-dictated susceptibility.

Maryland, Pennsylvania, Virginia, West Virginia↗
USGS2024

Detection of prions from spiked and free-ranging carnivore feces

Chronic wasting disease (CWD) is a highly contagious, fatal neurodegenerative disease caused by infectious prions (PrP CWD ) affecting wild and captive cervids. Although experimental feeding studies have demonstrated prions in feces of crows ( Corvus brachyrhynchos ), coyotes ( Canis latrans ), and cougars ( Puma concolor ), the role of scavengers and predators in CWD epidemiology remains poorly understood. Here we applied the real-time quaking-induced conversion (RT-QuIC) assay to detect PrP CWD in feces from cervid consumers, to advance surveillance approaches, which could be used to improve disease research and adaptive management of CWD. We assessed recovery and detection of PrP CWD by experimental spiking of PrP CWD into carnivore feces from 9 species sourced from CWD-free populations or captive facilities. We then applied this technique to detect PrP CWD from feces of predators and scavengers in free-ranging populations. Our results demonstrate that spiked PrP CWD is detectable from feces of free-ranging mammalian and avian carnivores using RT-QuIC. Results show that PrP CWD acquired in natural settings is detectable in feces from free-ranging carnivores, and that PrP CWD rates of detection in carnivore feces reflect relative prevalence estimates observed in the corresponding cervid populations. This study adapts an important diagnostic tool for CWD, allowing investigation of the epidemiology of CWD at the community-level.

Scientific Reports↗
USGS2012

Emerging prion disease drives host selection in a wildlife population

Infectious diseases are increasingly recognized as an important force driving population dynamics, conservation biology, and natural selection in wildlife populations. Infectious agents have been implicated in the decline of small or endangered populations and may act to constrain population size, distribution, growth rates, or migration patterns. Further, diseases may provide selective pressures that shape the genetic diversity of populations or species. Thus, understanding disease dynamics and selective pressures from pathogens is crucial to understanding population processes, managing wildlife diseases, and conserving biological diversity. There is ample evidence that variation in the prion protein gene (PRNP) impacts host susceptibility to prion diseases. Still, little is known about how genetic differences might influence natural selection within wildlife populations. Here we link genetic variation with differential susceptibility of white-tailed deer to chronic wasting disease (CWD), with implications for fitness and disease-driven genetic selection. We developed a single nucleotide polymorphism (SNP) assay to efficiently genotype deer at the locus of interest (in the 96th codon of the PRNP gene). Then, using a Bayesian modeling approach, we found that the more susceptible genotype had over four times greater risk of CWD infection; and, once infected, deer with the resistant genotype survived 49% longer (8.25 more months). We used these epidemiological parameters in a multi-stage population matrix model to evaluate relative fitness based on genotype-specific population growth rates. The differences in disease infection and mortality rates allowed genetically resistant deer to achieve higher population growth and obtain a long-term fitness advantage, which translated into a selection coefficient of over 1% favoring the CWD-resistant genotype. This selective pressure suggests that the resistant allele could become dominant in the population within an evolutionarily short time frame. Our work provides a rare example of a quantifiable disease-driven selection process in a wildlife population, demonstrating the potential for infectious diseases to alter host populations. This will have direct bearing on the epidemiology, dynamics, and future trends in CWD transmission and spread. Understanding genotype-specific epidemiology will improve predictive models and inform management strategies for CWD-affected cervid populations.

Ecological Applications↗
USGS2023

Ticks harbor and excrete chronic wasting disease prions

Chronic wasting disease (CWD) is a fatal neurodegenerative disease caused by infectious prions (PrP CWD ) affecting cervids. Circulating PrP CWD in blood may pose a risk for indirect transmission by way of hematophagous ectoparasites acting as mechanical vectors. Cervids can carry high tick infestations and exhibit allogrooming, a common tick defense strategy between conspecifics. Ingestion of ticks during allogrooming may expose naïve animals to CWD, if ticks harbor PrP CWD . This study investigates whether ticks can harbor transmission-relevant quantities of PrP CWD by combining experimental tick feeding trials and evaluation of ticks from free-ranging white-tailed deer ( Odocoileus virginianus ). Using the real-time quaking-induced conversion (RT-QuIC) assay, we show that black-legged ticks ( Ixodes scapularis ) fed PrP CWD -spiked blood using artificial membranes ingest and excrete PrP CWD . Combining results of RT-QuIC and protein misfolding cyclic amplification, we detected seeding activity from 6 of 15 (40%) pooled tick samples collected from wild CWD-infected white-tailed deer. Seeding activities in ticks were analogous to 10–1000 ng of CWD-positive retropharyngeal lymph node collected from deer upon which they were feeding. Estimates revealed a median infectious dose range of 0.3–42.4 per tick, suggesting that ticks can take up transmission-relevant amounts of PrP CWD and may pose a CWD risk to cervids.

Wisconsin↗
USGS2016

Seeded amplification of chronic wasting disease prions in nasal brushings and recto-anal mucosal associated lymphoid tissues from elk by real time quaking-induced conversion

Chronic wasting disease (CWD), a transmissible spongiform encephalopathy of cervids, was first documented nearly 50 years ago in Colorado and Wyoming and has since been detected across North America and the Republic of Korea. The expansion of this disease makes the development of sensitive diagnostic assays and antemortem sampling techniques crucial for the mitigation of its spread; this is especially true in cases of relocation/reintroduction or prevalence studies of large or protected herds, where depopulation may be contraindicated. This study evaluated the sensitivity of the real-time quaking-induced conversion (RT-QuIC) assay of recto-anal mucosa-associated lymphoid tissue (RAMALT) biopsy specimens and nasal brushings collected antemortem. These findings were compared to results of immunohistochemistry (IHC) analysis of ante- and postmortem samples. RAMALT samples were collected from populations of farmed and free-ranging Rocky Mountain elk ( Cervus elaphus nelsoni ; n = 323), and nasal brush samples were collected from a subpopulation of these animals ( n = 205). We hypothesized that the sensitivity of RT-QuIC would be comparable to that of IHC analysis of RAMALT and would correspond to that of IHC analysis of postmortem tissues. We found RAMALT sensitivity (77.3%) to be highly correlative between RT-QuIC and IHC analysis. Sensitivity was lower when testing nasal brushings (34%), though both RAMALT and nasal brush test sensitivities were dependent on both the PRNP genotype and disease progression determined by the obex score. These data suggest that RT-QuIC, like IHC analysis, is a relatively sensitive assay for detection of CWD prions in RAMALT biopsy specimens and, with further investigation, has potential for large-scale and rapid automated testing of antemortem samples for CWD.

Journal of Clinical Microbiology↗
USGS2013

Red-backed vole brain promotes highly efficient in vitro amplification of abnormal prion protein from macaque and human brains infected with variant Creutzfeldt-Jakob disease agent.

Rapid antemortem tests to detect individuals with transmissible spongiform encephalopathies (TSE) would contribute to public health. We investigated a technique known as protein misfolding cyclic amplification (PMCA) to amplify abnormal prion protein (PrP TSE ) from highly diluted variant Creutzfeldt-Jakob disease (vCJD)-infected human and macaque brain homogenates, seeking to improve the rapid detection of PrP TSE in tissues and blood. Macaque vCJD PrP TSE did not amplify using normal macaque brain homogenate as substrate (intraspecies PMCA). Next, we tested interspecies PMCA with normal brain homogenate of the southern red-backed vole (RBV), a close relative of the bank vole, seeded with macaque vCJD PrP TSE . The RBV has a natural polymorphism at residue 170 of the PrP-encoding gene (N/N, S/S, and S/N). We investigated the effect of this polymorphism on amplification of human and macaque vCJD PrP TSE . Meadow vole brain (170N/N PrP genotype) was also included in the panel of substrates tested. Both humans and macaques have the same 170S/S PrP genotype. Macaque PrP TSE was best amplified with RBV 170S/S brain, although 170N/N and 170S/N were also competent substrates, while meadow vole brain was a poor substrate. In contrast, human PrP TSE demonstrated a striking narrow selectivity for PMCA substrate and was successfully amplified only with RBV 170S/S brain. These observations suggest that macaque PrP TSE was more permissive than human PrP TSE in selecting the competent RBV substrate. RBV 170S/S brain was used to assess the sensitivity of PMCA with PrP TSE from brains of humans and macaques with vCJD. PrP TSE signals were reproducibly detected by Western blot in dilutions through 10 -12 of vCJD-infected 10% brain homogenates. This is the first report showing PrP TSE from vCJD-infected human and macaque brains efficiently amplified with RBV brain as the substrate. Based on our estimates, PMCA showed a sensitivity that might be sufficient to detect PrP TSE in vCJD-infected human and macaque blood.

PLoS ONE↗
USGS2016

Antemortem detection of chronic wasting disease prions in nasal brush collections and rectal biopsies from white-tailed deer by real time quaking-induced conversion

Chronic wasting disease (CWD), a transmissible spongiform encephalopathy of cervids, was first documented nearly 50 years ago in Colorado and Wyoming and has since spread to cervids in 23 states, two Canadian provinces, and the Republic of Korea. The expansion of this disease makes the development of sensitive diagnostic assays and antemortem sampling techniques crucial for the mitigation of its spread; this is especially true in cases of relocation/reintroduction of farmed or free-ranging deer and elk or surveillance studies of private or protected herds, where depopulation is contraindicated. This study sought to evaluate the sensitivity of the real-time quaking-induced conversion (RT-QuIC) assay by using recto-anal mucosa-associated lymphoid tissue (RAMALT) biopsy specimens and nasal brush samples collected antemortem from farmed white-tailed deer ( n = 409). Antemortem findings were then compared to results from ante- and postmortem samples (RAMALT, brainstem, and medial retropharyngeal lymph nodes) evaluated by using the current gold standard in vitro assay, immunohistochemistry (IHC) analysis. We hypothesized that the sensitivity of RT-QuIC would be comparable to IHC analysis in antemortem tissues and would correlate with both the genotype and the stage of clinical disease. Our results showed that RAMALT testing by RT-QuIC assay had the highest sensitivity (69.8%) compared to that of postmortem testing, with a specificity of >93.9%. These data suggest that RT-QuIC, like IHC analysis, is an effective assay for detection of PrP CWD in rectal biopsy specimens and other antemortem samples and, with further research to identify more sensitive tissues, bodily fluids, or experimental conditions, has potential for large-scale and rapid automated testing for CWD diagnosis.

Journal of Clinical Microbiology↗
USGS2022

Susceptibility of beavers to chronic wasting disease

Chronic wasting disease (CWD) is a contagious, fatal, neurodegenerative prion disease of cervids. The expanding geographical range and rising prevalence of CWD are increasing the risk of pathogen transfer and spillover of CWD to non-cervid sympatric species. As beavers have close contact with environmental and food sources of CWD infectivity, we hypothesized that they may be susceptible to CWD prions. We evaluated the susceptibility of beavers to prion diseases by challenging transgenic mice expressing beaver prion protein (tgBeaver) with five strains of CWD, four isolates of rodent-adapted prions and one strain of Creutzfeldt–Jakob disease. All CWD strains transmitted to the tgBeaver mice, with attack rates highest from moose CWD and the 116AG and H95+ strains of deer CWD. Mouse-, rat-, and especially hamster-adapted prions were also transmitted with complete attack rates and short incubation periods. We conclude that the beaver prion protein is an excellent substrate for sustaining prion replication and that beavers are at risk for CWD pathogen transfer and spillover.

Biology↗
USGS2025

Characterization of the long-distance dispersal kernel of white-tailed deer and evaluating its impact on chronic wasting disease spread in Wisconsin

Chronic wasting disease (CWD) is a fatal neurodegenerative disease infecting cervids. It is highly contagious and caused by misfolded prions that propagate via templated conformational conversion of the cervid’s normal prion protein. Prevalence of CWD in free-ranging deer in North America is mostly low, but in some regions local prevalence has reached 80%. CWD prions can be transmitted via direct contact with infected individuals or indirectly through the environment. Infected individuals shed prions through feces, urine, saliva or carcasses, and prions have long environmental persistence. Long-distance dispersal of infected deer poses a significant risk for CWD spread. We propose an integrodifference equation (IDE) model to capture CWD dynamics and the consequences of long-distance dispersal behavior in white-tailed deer (WTD, Odocoileus virginianus ). A diffusion-settling model characterizes long-distance dispersal kernels, accommodating hypothetical dispersal behaviors through time-dependent settling rate functions. Three new closed-form dispersal kernels are approximated using Laplace’s method and parameterized with GPS location data collected from WTD in Wisconsin, USA. Settling rates reflecting ongoing sensitivity to stimuli which prompt deer to disperse from their natal home range give the most supported long-distance dispersal kernel. Impact of long-distance dispersal on CWD spread is quantified using the IDE model. At high population densities, long-distance dispersal can magnify CWD spread by a factor of four. At lower population densities single infected individuals cannot initiate an outbreak, but CWD may still spread due to the accumulation of environmental hazard from prions behind the wave of invasion, possibly presenting substantial management challenges.

Wisconsin↗
USGS2022

Informing surveillance through the characterization of outbreak potential of chronic wasting disease in white-tailed deer

Understanding the role that an environmental prion reservoir plays in the outbreak dynamics of chronic wasting disease (CWD) in free ranging white-tailed deer ( Odocoileus virginianus ) is critical for the allocation of disease surveillance resources by state and provincial wildlife agencies. We hypothesized that demographic, ecological, and epidemiological configurations naturally attenuate epidemic risk despite the introduction of infectious prions into a susceptible population of deer, but the magnitude of infectious prions in the environmental prion reservoir complicate outbreak expectations. We developed a Susceptible-Latent-Exposed-Infective (SLEI) compartment model to represent the dynamics of CWD epidemics in free-ranging white-tailed deer, then used the basic reproductive ratio ( R 0 "> R0 ) to pinpoint counties under which pathogenic introduction (transport of infectious bodily fluids, tissues, and carcasses through natural or anthropogenic means) naturally produced (or failed to produce) an epidemic. We found that the outlook for an epidemic hinged on transmission rates, the magnitude of environmental contamination, and system type (density-, frequency-, or density/frequency-dependent). CWD can persistently infect individuals living in a contaminated environment even if direct transmission is insufficient to sustain circulation. Theoretical results show that transmission of CWD cannot be exclusively density dependent, and must behave as either a mix between frequency and density dependent, or strictly frequency dependent. While the compartment model is a simplistic representation of reality and did not contain many complicating biological considerations, it was immediately useful in hypothesis generation, motivating the collection of additional data for use in more biologically detailed models, and in the allocation of finite surveillance resources to place emphasis on data collection in areas where an introduction of infectious prions is comparatively more likely to result in an epidemic.

Ecological Modelling↗
USGS2024

Validation of a real-time quaking-induced conversion (RT-QuIC) assay protocol to detect chronic wasting disease using rectal mucosa of naturally infected, pre-clinical white-tailed deer (Odocoileus virginianus)

Chronic wasting disease (CWD) is a fatal prion disease of cervids spreading across North America. More effective mitigation efforts may require expansion of the available toolkit to include new methods that provide earlier antemortem detection, higher throughput, and less expense than current immunohistochemistry (IHC) methods. The rectal mucosa near the rectoanal junction is a site of early accumulation of CWD prions and is safely sampled in living animals by pinch biopsy. A fluorescence-based, 96-well format, protein-aggregation assay-the real-time quaking-induced conversion (RT-QuIC) assay-is capable of ultra-sensitive detection of CWD prions. Notably, the recombinant protein substrate is crucial to the assay's performance and is now commercially available. In this blinded independent study, the preclinical diagnostic performance of a standardized RT-QuIC protocol using a commercially sourced substrate (MNPROtein) and a laboratory-produced substrate was studied using mock biopsy samples of the rectal mucosa from 284 white-tailed deer ( Odocoileus virginianus ). The samples were from a frozen archive of intact rectoanal junctions collected at depopulations of farmed herds positive for CWD in the United States. All deer were pre-clinical at the time of depopulation and infection status was established from the regulatory record, which evaluated the medial retropharyngeal lymph nodes (MRPLNs) and obex by CWD-IHC. A pre-analytic sample precipitation step was found to enhance the protocol's detection limit. Performance metrics were influenced by the choice of RT-QuIC diagnostic cut points (minimum number of positive wells and assay time) and by deer attributes (preclinical infection stage and prion protein genotype). The peak overall diagnostic sensitivities of the protocol were similar for both substrates (MNPROtein, 76.8%; laboratory-produced, 73.2%), though each was achieved at different cut points. Preclinical infection stage and prion protein genotype at codon 96 (G = glycine, S = serine) were primary predictors of sensitivity. The diagnostic sensitivities in late preclinical infections (CWD-IHC positive MPRLNs and obex) were similar, ranging from 96% in GG96 deer to 80% in xS96 deer (x = G or S). In early preclinical infections (CWD-IHC positive MRPLNs only), the diagnostic sensitivity was 64-71% in GG96 deer but only 25% in xS96 deer. These results demonstrate that this standardized RT-QuIC protocol for rectal biopsy samples using a commercial source of substrate produced stratified diagnostic sensitivities similar to or greater than those reported for CWD-IHC but in less than 30 hours of assay time and in a 96-well format. Notably, the RT-QuIC protocol used herein represents a standardization of protocols from several previous studies. Alignment of the sensitivities across these studies suggests the diagnostic performance of the assay is robust given quality reagents, optimized diagnostic criteria, and experienced staff.

PLoS ONE↗
USGS2026

Modeling chronic wasting disease transmission risk in mule deer related to habitat characteristics

Chronic wasting disease (CWD) is a prion disease of cervids that spreads to uninfected individuals through direct transmission (contact with infected individuals), vertical transmission (from mother to offspring), or indirect transmission (exposure to contaminated environments). The risk of indirect transmission is unevenly distributed on the landscape, and risk levels are expected to be controlled by patterns of habitat use by infected and uninfected individuals as well as environmental properties that alter the length of time prions remain infectious and available for uptake. Despite evidence from controlled or laboratory studies identifying environmental properties likely to affect patterns of CWD prion locations on the landscape, it remains difficult to connect mechanisms to realized increased or decreased risk of disease transmission, and few studies have attempted to detect patterns of different CWD risk in different environments. Using data from GPS-collared mule deer in Wyoming that were CWD-tested annually, we constructed models predicting annual probability of disease transmission contingent on environmental properties extracted from GPS use points. We compared models that emphasized different pathways of disease transmission by including or excluding sets of covariates that described deer density, habitat selection, and covariates expected to affect prion persistence in the environment. Results indicated that key habitat characteristics often selected by mule deer, such as proximity to secondary roads, were also associated with higher risk of testing positive for CWD, which supports the hypothesis that disease risk was correlated to patterns of habitat use by deer. We also found increased risk associated with spatial properties that were not selected-for by deer, such as areas where topography collects moisture, suggesting that prion retention mechanisms also play a role in risk. Incorporating these spatially-varying risk factors into our understanding of CWD transmission and outbreak progression can support managers in designing data collection and disease management strategies.

Wyoming↗
USGS2025

Overview of North American isolates of chronic wasting disease used for strain research

Chronic Wasting Disease (CWD) is a prion disease that affects Cervidae species, and is the only known prion disease transmitted among wildlife species. The key pathological feature is the conversion of the normal prion protein (PrP C ) misfolding into abnormal forms (PrP Sc ), triggering the onset of CWD infections. The misfolding can generate distinct PrP Sc conformations (strains) giving rise to diverse disease phenotypes encompassing pathology, incubation period, and clinical signs. These phenotypes operationally define distinct prion strains, a pivotal element in monitoring CWD spread and zoonotic potential—a complex endeavor compounded by defining and tracking CWD strains. This review pursues a tripartite objective: 1. to address the intricate challenges inherent in ongoing CWD strain classification; 2. to provide an overview of the known CWD-infected isolates, the strains they represent and their passage history; and 3. to describe the spatial diversity of CWD strains in North America, enriching our understanding of CWD strain dynamics. By delving into these dimensions, this review sheds light on the intricate interplay among polymorphisms, biochemical properties, and clinical expressions of CWD. This endeavor aims to elevate the trajectory of CWD research, advancing our insight into prion disease.

Pathogens↗