Media Contact: Steve Lightfoot, TPWD, 512-389-4701, steve.lightfoot@tpwd.texas.gov Callie McNulty, TAHC, 512-719-0728, callie.mcnulty@tahc.texas.gov

July 1, 2015

Chronic Wasting Disease Detected in Medina County Captive Deer

AUSTIN – A two-year-old white-tailed deer in a Medina County deer breeding facility has been confirmed positive for Chronic Wasting Disease (CWD). This is the first case of CWD detected in captive white-tailed deer in Texas. CWD was first detected in Texas in 2012 in free-ranging mule deer in the Hueco Mountains in far West Texas.

The Medina County tissue samples submitted by the breeder facility in early June as part of routine deer mortality surveillance revealed the presence of CWD during testing at the Texas A&M Veterinary Medical Diagnostic Laboratory (TVMDL) in College Station. The National Veterinary Services Laboratory in Ames, Iowa, confirmed the findings on Tuesday, June 30.

An epidemiological investigation to determine the extent of the disease, assess risks to Texas’ free ranging deer and protect the captive deer and elk breeding industry is being led by the Texas Animal Health Commission (TAHC), in coordination with the Texas Parks and Wildlife Department (TPWD) and U.S. Department of Agriculture’s Animal and Plant Health Inspection Service Veterinary Services (USDA/APHIS/VS).

Officials have taken immediate action to secure all cervids at the Medina County breeder facility with plans to conduct additional investigation for CWD. In addition, those breeder facilities that have received deer from the Medina County facility or shipped deer to that facility during the last two years are under movement restrictions and cannot move or release cervids at this time. TPWD is disallowing liberation of captive deer from all breeder facilities into the wild at this time pending further review. Additional measures to further minimize risk of CWD spreading into Texas’ free-ranging white-tailed deer herd, and to protect the captive deer breeding industry, will be considered.

“This is a terribly unfortunate development that we are committed to addressing as proactively, comprehensively, and expeditiously as possible. The health of our state’s wild and captive deer herds, as well as affiliated hunting, wildlife, and rural based economies, are vitally important to Texas hunters, communities, and landowners. As such, our primary objectives are to determine the source of the disease and to identify other deer breeding facilities and release sites that may have received deer from affected facilities,” said Carter Smith, TPWD Executive Director. “Working collaboratively with experts in the field we have developed protocols to address CWD, and our implementation efforts are already well under way.”

The TPWD and the TAHC CWD Management Plan will guide the State’s response to this incident. The plan was developed by the State’s CWD Task Force, which is comprised of deer and elk breeders, wildlife biologists, veterinarians and other animal-health experts from TPWD, TAHC, TVMDL, Department of State Health Services, Texas A&M College of Veterinary Medicine, and USDA.

Since 2002, the state has conducted surveillance throughout Texas for the disease. More than 34,000 samples collected from hunter-harvested and road kill deer have been tested for CWD.

Although animal health and wildlife officials cannot say how long or to what extent the disease has been present in the Medina County deer breeding facility, the breeder has had an active CWD surveillance program since 2006 with no positives detected until now.

“We are working with experts at the local, state and federal level, to determine the extent of this disease, and respond appropriately to limit further transmission,” said Dr. Andy Schwartz, TAHC Epidemiologist and Assistant Executive Director. “Strong public awareness and the continued support of the cervid industry is paramount to the success of controlling CWD in Texas.”

The disease was first recognized in 1967 in captive mule deer in Colorado. CWD has also been documented in captive and/or free-ranging deer in 23 states and 2 Canadian provinces. CWD among cervids is a progressive, fatal disease that commonly results in altered behavior as a result of microscopic changes made to the brain of affected animals. An animal may carry the disease for years without outward indication, but in the latter stages, signs may include listlessness, lowering of the head, weight loss, repetitive walking in set patterns, and a lack of responsiveness. To date there is no evidence that CWD poses a risk to humans or non-cervids. However, as a precaution, the U.S. Centers for Disease Control and the World Health Organization recommend not to consume meat from infected animals.

More information on CWD can be found on TPWD’s website, www.tpwd.texas.gov/CWD or at the Chronic Wasting Disease Alliance website, www.cwd-info.org.

More information about the TAHC CWD program may be found at http://tahc.state.tx.us/animal_health/cwd/cwd.html.

2015-07-01

http://tpwd.texas.gov/newsmedia/releases/?req=20150701a&nrtype=all&nrspan=2015&nrsearch=

*** LATE-BREAKING ABSTRACTS PRION 2015 CONFERENCE ***

O18

Zoonotic Potential of CWD Prions

Liuting Qing1, Ignazio Cali1,2, Jue Yuan1, Shenghai Huang3, Diane Kofskey1, Pierluigi Gambetti1, Wenquan Zou1, Qingzhong Kong1 1Case Western Reserve University, Cleveland, Ohio, USA, 2Second University of Naples, Naples, Italy, 3Encore Health Resources, Houston, Texas, USA

Chronic wasting disease (CWD) is a widespread and expanding prion disease in free-ranging and captive cervid species in North America. The zoonotic potential of CWD prions is a serious public health concern. Current literature generated with in vitro methods and in vivo animal models (transgenic mice, macaques and squirrel monkeys) reports conflicting results. The susceptibility of human CNS and peripheral organs to CWD prions remains largely unresolved. In our earlier bioassay experiments using several humanized transgenic mouse lines, we detected protease-resistant PrPSc in the spleen of two out of 140 mice that were intracerebrally inoculated with natural CWD isolates, but PrPSc was not detected in the brain of the same mice. Secondary passages with such PrPSc-positive CWD-inoculated humanized mouse spleen tissues led to efficient prion transmission with clear clinical and pathological signs in both humanized and cervidized transgenic mice. Furthermore, a recent bioassay with natural CWD isolates in a new humanized transgenic mouse line led to clinical prion infection in 2 out of 20 mice. ***These results indicate that the CWD prion has the potential to infect human CNS and peripheral lymphoid tissues and that there might be asymptomatic human carriers of CWD infection.

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***These results indicate that the CWD prion has the potential to infect human CNS and peripheral lymphoid tissues and that there might be asymptomatic human carriers of CWD infection.***

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P.105: RT-QuIC models trans-species prion transmission

Kristen Davenport, Davin Henderson, Candace Mathiason, and Edward Hoover Prion Research Center; Colorado State University; Fort Collins, CO USA

The propensity for trans-species prion transmission is related to the structural characteristics of the enciphering and heterologous PrP, but the exact mechanism remains mostly mysterious. Studies of the effects of primary or tertiary prion protein structures on trans-species prion transmission have relied primarily upon animal bioassays, making the influence of prion protein structure vs. host co-factors (e.g. cellular constituents, trafficking, and innate immune interactions) difficult to dissect. As an alternative strategy, we used real-time quakinginduced conversion (RT-QuIC) to investigate trans-species prion conversion.

To assess trans-species conversion in the RT-QuIC system, we compared chronic wasting disease (CWD) and bovine spongiform encephalopathy (BSE) prions, as well as feline CWD (fCWD) and feline spongiform encephalopathy (FSE). Each prion was seeded into each host recombinant PrP (full-length rPrP of white-tailed deer, bovine or feline). We demonstrated that fCWD is a more efficient seed for feline rPrP than for white-tailed deer rPrP, which suggests adaptation to the new host.

Conversely, FSE maintained sufficient BSE characteristics to more efficiently convert bovine rPrP than feline rPrP. Additionally, human rPrP was competent for conversion by CWD and fCWD. ***This insinuates that, at the level of protein:protein interactions, the barrier preventing transmission of CWD to humans is less robust than previously estimated.

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***This insinuates that, at the level of protein:protein interactions, the barrier preventing transmission of CWD to humans is less robust than previously estimated.***

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cwd environmental load factor in the land and surrounding plants and objects.

transportation of cervids and HUMANS from cwd zone should be regarded as a great risk factor, and environmental contamination.

PL1

Using in vitro prion replication for high sensitive detection of prions and prionlike proteins and for understanding mechanisms of transmission.

Claudio Soto

Mitchell Center for Alzheimer's diseases and related Brain disorders, Department of Neurology, University of Texas Medical School at Houston.

Prion and prion-like proteins are misfolded protein aggregates with the ability to selfpropagate to spread disease between cells, organs and in some cases across individuals. I n T r a n s m i s s i b l e s p o n g i f o r m encephalopathies (TSEs), prions are mostly composed by a misfolded form of the prion protein (PrPSc), which propagates by transmitting its misfolding to the normal prion protein (PrPC). The availability of a procedure to replicate prions in the laboratory may be important to study the mechanism of prion and prion-like spreading and to develop high sensitive detection of small quantities of misfolded proteins in biological fluids, tissues and environmental samples. Protein Misfolding Cyclic Amplification (PMCA) is a simple, fast and efficient methodology to mimic prion replication in the test tube. PMCA is a platform technology that may enable amplification of any prion-like misfolded protein aggregating through a seeding/nucleation process. In TSEs, PMCA is able to detect the equivalent of one single molecule of infectious PrPSc and propagate prions that maintain high infectivity, strain properties and species specificity. Using PMCA we have been able to detect PrPSc in blood and urine of experimentally infected animals and humans affected by vCJD with high sensitivity and specificity. Recently, we have expanded the principles of PMCA to amplify amyloid-beta (Aβ) and alphasynuclein (α-syn) aggregates implicated in Alzheimer's and Parkinson's diseases, respectively. Experiments are ongoing to study the utility of this technology to detect Aβ and α-syn aggregates in samples of CSF and blood from patients affected by these diseases.

***Recently, we have been using PMCA to study the role of environmental prion contamination on the horizontal spreading of TSEs. These experiments have focused on the study of the interaction of prions with plants and environmentally relevant surfaces. Our results show that plants (both leaves and roots) bind tightly to prions present in brain extracts and excreta (urine and feces) and retain even small quantities of PrPSc for long periods of time. Strikingly, ingestion of prioncontaminated leaves and roots produced disease with a 100% attack rate and an incubation period not substantially longer than feeding animals directly with scrapie brain homogenate. Furthermore, plants can uptake prions from contaminated soil and transport them to different parts of the plant tissue (stem and leaves). Similarly, prions bind tightly to a variety of environmentallyrelevant surfaces, including stones, wood, metals, plastic, glass, cement, etc. Prion contaminated surfaces efficiently transmit prion disease when these materials were directly injected into the brain of animals and strikingly when the contaminated surfaces were just placed in the animal cage. These findings demonstrate that environmental materials can efficiently bind infectious prions and act as carriers of infectivity, suggesting that they may play an important role in the horizontal transmission of the disease.

Since its invention 13 years ago, PMCA has helped to answer fundamental questions of prion propagation and has broad applications in research areas including the food industry, blood bank safety and human and veterinary disease diagnosis.

https://prion2015.files.wordpress.com/2015/05/programguide1.pdf

Wednesday, June 10, 2015

Zoonotic Potential of CWD Prions

LATE-BREAKING ABSTRACTS

http://chronic-wasting-disease.blogspot.com/2015/06/zoonotic-potential-of-cwd-prions.html

O.05: Transmission of prions to primates after extended silent incubation periods: Implications for BSE and scrapie risk assessment in human populations

Emmanuel Comoy, Jacqueline Mikol, Val erie Durand, Sophie Luccantoni, Evelyne Correia, Nathalie Lescoutra, Capucine Dehen, and Jean-Philippe Deslys Atomic Energy Commission; Fontenay-aux-Roses, France

Prion diseases (PD) are the unique neurodegenerative proteinopathies reputed to be transmissible under field conditions since decades. The transmission of Bovine Spongiform Encephalopathy (BSE) to humans evidenced that an animal PD might be zoonotic under appropriate conditions. Contrarily, in the absence of obvious (epidemiological or experimental) elements supporting a transmission or genetic predispositions, PD, like the other proteinopathies, are reputed to occur spontaneously (atpical animal prion strains, sporadic CJD summing 80% of human prion cases). Non-human primate models provided the first evidences supporting the transmissibiity of human prion strains and the zoonotic potential of BSE. Among them, cynomolgus macaques brought major information for BSE risk assessment for human health (Chen, 2014), according to their phylogenetic proximity to humans and extended lifetime. We used this model to assess the zoonotic potential of other animal PD from bovine, ovine and cervid origins even after very long silent incubation periods. *** We recently observed the direct transmission of a natural classical scrapie isolate to macaque after a 10-year silent incubation period, ***with features similar to some reported for human cases of sporadic CJD, albeit requiring fourfold longe incubation than BSE. Scrapie, as recently evoked in humanized mice (Cassard, 2014), ***is the third potentially zoonotic PD (with BSE and L-type BSE), ***thus questioning the origin of human sporadic cases. We will present an updated panorama of our different transmission studies and discuss the implications of such extended incubation periods on risk assessment of animal PD for human health.

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***thus questioning the origin of human sporadic cases...TSS

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https://prion2015.files.wordpress.com/2015/05/prion2015abstracts.pdf

Friday, January 30, 2015

*** Scrapie: a particularly persistent pathogen ***

http://transmissiblespongiformencephalopathy.blogspot.com/2015/01/scrapie-particularly-persistent-pathogen.html

Tuesday, December 16, 2014 Scrapie from sheep could infect humans with 'mad cow disease', study finds

Evidence for zoonotic potential of ovine scrapie prions

Hervé Cassard,1, n1 Juan-Maria Torres,2, n1 Caroline Lacroux,1, Jean-Yves Douet,1, Sylvie L. Benestad,3, Frédéric Lantier,4, Séverine Lugan,1, Isabelle Lantier,4, Pierrette Costes,1, Naima Aron,1, Fabienne Reine,5, Laetitia Herzog,5, Juan-Carlos Espinosa,2, Vincent Beringue5, & Olivier Andréoletti1, Affiliations Contributions Corresponding author Journal name: Nature Communications Volume: 5, Article number: 5821 DOI: doi:10.1038/ncomms6821 Received 07 August 2014 Accepted 10 November 2014 Published 16 December 2014 Article tools Citation Reprints Rights & permissions Article metrics

Abstract

Although Bovine Spongiform Encephalopathy (BSE) is the cause of variant Creutzfeldt Jakob disease (vCJD) in humans, the zoonotic potential of scrapie prions remains unknown. Mice genetically engineered to overexpress the human prion protein (tgHu) have emerged as highly relevant models for gauging the capacity of prions to transmit to humans. These models can propagate human prions without any apparent transmission barrier and have been used used to confirm the zoonotic ability of BSE. Here we show that a panel of sheep scrapie prions transmit to several tgHu mice models with an efficiency comparable to that of cattle BSE. ***The serial transmission of different scrapie isolates in these mice led to the propagation of prions that are phenotypically identical to those causing sporadic CJD (sCJD) in humans. ***These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions.

Subject terms: Biological sciences• Medical research At a glance

http://www.nature.com/ncomms/2014/141216/ncomms6821/full/ncomms6821.html

see more here ;

http://www.nature.com/ncomms/2014/141216/ncomms6821/extref/ncomms6821-s1.pdf

Wednesday, March 18, 2015

Chronic Wasting Disease CWD Confirmed Texas Trans Pecos March 18, 2015

http://chronic-wasting-disease.blogspot.com/2015/03/chronic-wasting-disease-cwd-confirmed.html

Wednesday, March 25, 2015

Chronic Wasting Disease CWD Cases Confirmed In New Mexico 2013 and 2014 UPDATE 2015

http://chronic-wasting-disease.blogspot.com/2015/03/chronic-wasting-disease-cwd-cases.html

Friday, May 22, 2015

Chronic Wasting Disease and Program Updates - 2014 NEUSAHA Annual Meeting 12-14 May 2014