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Journal of Virology, January 2006, p. 322-331, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.322-331.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Inactivation of Prions by Acidic Sodium Dodecyl Sulfate

David Peretz ,1,2,{dagger},{ddagger} Surachai Supattapone,1,2,{dagger},§ Kurt Giles,1,2,{dagger} Julie Vergara,1 Yevgeniy Freyman,1 Pierre Lessard,1 Jiri G. Safar,1,2 David V. Glidden,3 Charles McCulloch,3 Hoang-Oanh B. Nguyen,1 Michael Scott,1,2,|| Stephen J. DeArmond,1,4 and Stanley B. Prusiner1,2,5*

Institute for Neurodegenerative Diseases,1 Departments of Neurology,2 Epidemiology and Biostatistics,3 Pathology,4 Biochemistry and Biophysics, University of California San Francisco, San Francisco, California 941435

Received 14 March 2005/ Accepted 16 September 2005

Prompted by the discovery that prions become protease-sensitive after exposure to branched polyamine dendrimers in acetic acid (AcOH) (S. Supattapone, H. Wille, L. Uyechi, J. Safar, P. Tremblay, F. C. Szoka, F. E. Cohen, S. B. Prusiner, and M. R. Scott, J. Virol. 75:3453-3461, 2001), we investigated the inactivation of prions by sodium dodecyl sulfate (SDS) in weak acid. As judged by sensitivity to proteolytic digestion, the disease-causing prion protein (PrPSc) was denatured at room temperature by SDS at pH values of ≤4.5 or ≥10. Exposure of Sc237 prions in Syrian hamster brain homogenates to 1% SDS and 0.5% AcOH at room temperature resulted in a reduction of prion titer by a factor of ca. 107; however, all of the bioassay hamsters eventually developed prion disease. When various concentrations of SDS and AcOH were tested, the duration and temperature of exposure acted synergistically to inactivate both hamster Sc237 prions and human sporadic Creutzfeldt-Jakob disease (sCJD) prions. The inactivation of prions in brain homogenates and those bound to stainless steel wires was evaluated by using bioassays in transgenic mice. sCJD prions were more than 100,000 times more resistant to inactivation than Sc237 prions, demonstrating that inactivation procedures validated on rodent prions cannot be extrapolated to inactivation of human prions. Some procedures that significantly reduced prion titers in brain homogenates had a limited effect on prions bound to the surface of stainless steel wires. Using acidic SDS combined with autoclaving for 15 min, human sCJD prions bound to stainless steel wires were eliminated. Our findings form the basis for a noncorrosive system that is suitable for inactivating prions on surgical instruments, as well as on other medical and dental equipment.

* Corresponding author. Mailing address: Institute for Neurodegenerative Diseases, 513 Parnassus Ave., HSE-774, San Francisco, CA 94143-0518. Phone: (415) 476-4482. Fax: (415) 476-8386. E-mail: stanley{at}ind.ucsf.edu.

{dagger} D.P., S.S., and K.G. contributed equally to this study.

{ddagger} Present address: Chiron Corp., Emeryville, CA 94608-2916.

§ Present address: Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755.

|| Present address: Department of Zoology, University College, Belfield, Dublin 4, Ireland.

Journal of Virology, January 2006, p. 322-331, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.322-331.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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