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Journal of Virology, March 2006, p. 2106-2117, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2106-2117.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mouse-Adapted Scrapie Infection of SN56 Cells: Greater Efficiency with Microsome-Associated versus Purified PrP-res

Gerald S. Baron,1* Ana C. Magalhães,1,2 Marco A. M. Prado,2 and Byron Caughey1

Rocky Mountain Laboratories, Laboratory of Persistent Viral Diseases, NIAID, NIH, 903 S. 4th St., Hamilton, Montana 59840,1 Program of Molecular and Biochemical Pharmacology, Department of Pharmacology, ICB, Universidade Federal de Minas Gerais, Av. Antonio Carlos 6627, 31270-901, Brazil2

Received 2 September 2005/ Accepted 8 December 2005

The process by which transmissible spongiform encephalopathy agents, or prions, infect cells is unknown. We employed a new differentiable cell line (SN56) susceptible to infection with three mouse-adapted scrapie strains to gain insight into the cellular infection process. The effect of disease-associated PrP (PrP-res) association with microsomal membranes on infection efficiency was examined by comparing sustained PrP-res production in cells treated with either scrapie brain microsomes or purified, detergent-extracted PrP-res. When normalized for quantity of input PrP-res, scrapie brain microsomes induced dramatically enhanced persistent PrP-res formation compared to purified PrP-res. Infected SN56 cells released low levels of PrP-res into the culture supernatant, which also efficiently initiated infection in recipient cells. Interestingly, microsomes labeled with a fluorescent marker were internalized by SN56 cells in small vesicles, which were subsequently found in neuritic processes. When bound to culture wells to reduce internalization during the infection process, scrapie microsomes induced less long-term PrP-res production than suspended microsomes. Long-term differentiation of infected SN56 cells was accompanied by a decrease in PrP-res formation. Our observations provide evidence that infection of cells is aided by the association of PrP-res with membranes and/or other microsomal constituents.

* Corresponding author. Mailing address: Rocky Mountain Laboratories, Laboratory of Persistent Viral Diseases, NIAID, NIH, 903 S. 4th St., Hamilton, MT 59840. Phone: (406) 363-9485. Fax: (406) 363-9286. E-mail: gbaron{at}niaid.nih.gov.

Journal of Virology, March 2006, p. 2106-2117, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2106-2117.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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