Abstract

Chronic wasting disease (CWD) is a prion disease circulating in wild and farmed cervid populations throughout North America (United States and Canada), Europe (Finland, Norway, Sweden), and South Korea. CWD is a long-term threat to all cervid populations and to cervid hunting heritage, with the potential to cause substantial economic losses across multiple sectors. In North America, hunting and farming industries focused on the processing and consumption of white-tailed deer (WTD) venison are particularly vulnerable to CWD prion contamination, as millions of WTD are consumed annually. Real-time quaking-induced conversion (RT-QuIC) is a highly sensitive assay amplifying misfolded CWD prions in vitro and has facilitated CWD prion detection in a variety of tissues and excreta. To date, no study has comprehensively examined CWD prion content across bulk skeletal muscle tissues harvested from individual CWD infected WTD. Here, we use RT-QuIC to characterize prion-seeding activity in a variety of skeletal muscles from both wild and farmed CWD-positive WTD. We successfully detected CWD prions in muscles commonly used for consumption (e.g., backstrap, tenderloin, etc.) as well as within tongue and neck samples of WTD. Our results suggest that CWD prions are distributed across the skeletal muscles of infected WTD. We posit that RT-QuIC will be a useful tool for monitoring CWD prions in venison and that the method (with additional protocol optimization and high-throughput functionality) could be used to reduce and/or prevent CWD prions from entering animal and human food chains.

Highlights

  • Chronic wasting disease (CWD) is a prion disease circulating in wild and farmed cervid populations throughout North America (United States and Canada), Europe (Finland, Norway, Sweden), and South Korea

  • We investigated whether CWD prion deposition is limited to certain groups of muscles or if it is more generalized by using multiple white-tailed deer (WTD) skeletal muscle groups across the body, including muscles from the tongue, forelimb, backstrap, tenderloin, and hindlimb from both wild and farmed CWD positive animals independently determined by enzymelinked immunosorbent assay (ELISA) and/or IHC

  • In contrast to animals with official CWD-positive test results (i.e., ELISA and IHC), none of the muscle samples from CWD-negative animals showed statistically significant prion seeding activity in Real-time quaking-induced conversion (RT-QuIC) (Fig. 1b), despite one of eight wells crossing the threshold from a single animal (Fig. 1d)

Read more

Summary

Introduction

Chronic wasting disease (CWD) is a prion disease circulating in wild and farmed cervid populations throughout North America (United States and Canada), Europe (Finland, Norway, Sweden), and South Korea. Real-time quaking-induced conversion (RT-QuIC) is a highly sensitive assay amplifying misfolded CWD prions in vitro and has facilitated CWD prion detection in a variety of tissues and excreta. We use RT-QuIC to characterize prion-seeding activity in a variety of skeletal muscles from both wild and farmed CWD-positive WTD. In vitro experiments showed that CWD prions can convert human prion proteins into a misfolded and potentially disease-causing f­orm[5] For these reasons, as of 2020, both the Food and Drug Administration (FDA) and Food Safety and Inspection Service, United States Department of Agriculture (FSIS, USDA) consider venison from CWD-positive animals as adulterated and unsuitable for c­ onsumption[7,8]. Despite clear advantages of RT-QuIC as a screening ­method[9,31,32], no comprehensive reports are available for detecting CWD prions using RT-QuIC in skeletal muscle

Methods
Results
Conclusion

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.