Development of a Procedure for Prion Surveillance in the Laboratory Setting

Infectious prions readily adhere to common surfaces, retain infectivity, and are highly resistant to conventional decontamination, posing significant biosafety challenges in the medical and research environments. Recent occupational exposures underscore the urgency of improving safety measures. Here, we describe an approach combining foam-swab surface sampling and protein misfolding cyclic amplification to enhance prion surveillance. Our results demonstrate the ability to detect prions most relevant to human health directly from contaminated surfaces, even at 100 million-fold dilutions of the brain. We applied our method to assess the completeness of prion decontamination and show that high prion quantities can resist even approved inactivation methods. Finally, we applied our method in 2 real-world scenarios including the decommissioning and repurposing of a prion research facility and the active surveillance of residual prion contamination in an operational laboratory. Our methodology offers a robust and efficient tool for detecting residual prion contamination, enhancing laboratory safety.

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Publication Details

Journal
The Journal of Infectious Diseases
Published
2025-04-22
DOI
https://doi.org/10.1093/infdis/jiaf205
Primary Topic
Prion Diseases and Protein Misfolding
Type
article
Field-Weighted Citation Impact
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article

Development of a Procedure for Prion Surveillance in the Laboratory Setting

Damian Gorski, Fei Wang, Sandra Pritzkow, Ananya Tupaki‐Sreepurna et al.
The Journal of Infectious Diseases
Prion Diseases and Protein Misfolding
article

Development of a Procedure for Prion Surveillance in the Laboratory Setting

Damian Gorski, Fei Wang, Sandra Pritzkow, Ananya Tupaki‐Sreepurna, Claudio Soto, Isaac Schauer, Kane Spicker
article en

Abstract

Infectious prions readily adhere to common surfaces, retain infectivity, and are highly resistant to conventional decontamination, posing significant biosafety challenges in the medical and research environments. Recent occupational exposures underscore the urgency of improving safety measures. Here, we describe an approach combining foam-swab surface sampling and protein misfolding cyclic amplification to enhance prion surveillance. Our results demonstrate the ability to detect prions most relevant to human health directly from contaminated surfaces, even at 100 million-fold dilutions of the brain. We applied our method to assess the completeness of prion decontamination and show that high prion quantities can resist even approved inactivation methods. Finally, we applied our method in 2 real-world scenarios including the decommissioning and repurposing of a prion research facility and the active surveillance of residual prion contamination in an operational laboratory. Our methodology offers a robust and efficient tool for detecting residual prion contamination, enhancing laboratory safety.

The Journal of Infectious DiseasesVol. 232(6)
The University of Texas MD Anderson Cancer Center (US), The University of Texas Health Science Center (US), The University of Texas Health Science Center at Houston (US)
Openalex Percentile: Top 92%
Prion Diseases and Protein Misfolding
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