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BSE Infectivity Survives Burial for Five Years with Only Limited Spread

Overview
Journal Arch Virol
Specialty Microbiology
Date 2019 Feb 26
PMID 30799509
Citations 15
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Abstract

The carcasses of animals infected with bovine spongiform encephalopathy (BSE), scrapie or chronic wasting disease (CWD) that remain in the environment (exposed or buried) may continue to act as reservoirs of infectivity. We conducted two experiments under near-field conditions to investigate the survival and dissemination of BSE infectivity after burial in a clay or sandy soil. BSE infectivity was either contained within a bovine skull or buried as an uncontained bolus of BSE-infected brain. Throughout the five-year period of the experiment, BSE infectivity was recovered in similar amounts from heads exhumed annually from both types of soil. Very low levels of infectivity were detected in the soil immediately surrounding the heads, but not in samples remote from them. Similarly, there was no evidence of significant lateral movement of infectivity from the buried bolus over 4 years although there was a little vertical movement in both directions. However, bioassay analysis of limited numbers of samples of rain water that had drained through the bolus clay lysimeter indicated that infectivity was present in filtrates. sPMCA analysis also detected low levels of PrP in the filtrates up to 25 months following burial, raising the concern that leakage of infectivity into ground water could occur. We conclude that transmissible spongiform encephalopathy infectivity is likely to survive burial for long periods of time, but not to migrate far from the site of burial unless a vector or rain water drainage transports it. Risk assessments of contaminated sites should take these findings into account.

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References
1.
Taylor D . Inactivation of transmissible degenerative encephalopathy agents: A review. Vet J. 2000; 159(1):10-7. DOI: 10.1053/tvjl.1999.0406. View

2.
Somerville R, Oberthur R, Havekost U, MacDonald F, Taylor D, Dickinson A . Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J Biol Chem. 2002; 277(13):11084-9. DOI: 10.1074/jbc.M111766200. View

3.
Scudamore J, Trevelyan G, Tas M, Varley E, Hickman G . Carcass disposal: lessons from Great Britain following the foot and mouth disease outbreaks of 2001. Rev Sci Tech. 2003; 21(3):775-87. DOI: 10.20506/rst.21.3.1377. View

4.
Langeveld J, Wang J, van de Wiel D, Shih G, Garssen G, Bossers A . Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J Infect Dis. 2003; 188(11):1782-9. DOI: 10.1086/379664. View

5.
Feraudet C, Morel N, Simon S, Volland H, Frobert Y, Creminon C . Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J Biol Chem. 2004; 280(12):11247-58. DOI: 10.1074/jbc.M407006200. View