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Journal of Virology, April 2000, p. 3135-3140, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Amphotericin B Inhibits the Generation of the
Scrapie Isoform of the Prion Protein in Infected Cultures
Alain
Mangé,
Noriyuki
Nishida,
Ollivier
Milhavet,
Hilary E. M.
McMahon,
Danielle
Casanova, and
Sylvain
Lehmann*
Institut de Génétique Humaine,
CNRS U.P.R. 1142, 34396 Montpellier Cedex 5, France
Received 12 November 1999/Accepted 27 December 1999
Transmissible spongiform encephalopathies form a group of fatal
neurodegenerative disorders that have the unique property of being
infectious, sporadic, or genetic in origin. Although some doubts about
the nature of the responsible agent of these diseases remain, it is
clear that a protein called PrPSc plays a central role.
PrPSc is a conformational variant of PrPC, the
normal host protein. Polyene antibiotics such as amphotericin B have
been shown to delay the accumulation of PrPSc and to
increase the incubation time of the disease after experimental transmission in laboratory animals. Unlike for Congo red and sulfated polyanions, no effect of amphotericin B has been observed in infected cultures. We show here for the first time that amphotericin B can
inhibit PrPSc generation in scrapie-infected GT1-7 and N2a
cells. Its activity seems to be related to a modification of the
properties of detergent-resistant microdomains. These results provide
new insights into the mechanism of action of amphotericin B and confirm
the usefulness of infected cultures in the therapeutic research of
transmissible spongiform encephalopathies.
*
Corresponding author. Mailing address: CNRS, 141, rue
de la Cardonille, 34396 Montpellier Cedex 5, France. Phone: 33 (0)4 99 61 99 31. Fax: 33 (0)4 99 61 99 01. E-mail:
Sylvain.Lehmann{at}igh.cnrs.fr.
Journal of Virology, April 2000, p. 3135-3140, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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