Prion Therapy Inhibits Infection in Mice
Transmissible spongiform encephalopathies (TSEs) are characterized by malformed proteins that initiate deadly brain diseases such as scrapie in sheep, mad cow disease in cattle, and Creutzfeld-Jacob disease in humans. These so-called prion diseases have no cure, no treatment, and are always fatal.
Using scrapie-infected mice, researchers at the Rocky Mountain Laboratories (RML) of the National Institute of Allergy and Infectious Diseases have shown that degenerate phosphorothioate oligonucleotides (PS-ONs)—synthetic molecules related to natural nucleic acids—potently inhibit the accumulation of harmful abnormal protein and dramatically prolong the rodents’ lives. Typically, the abnormal proteins—thought to be prions—kill brain cells and cause death.
This new information points to a potential type of anti-TSE drug for at-risk animal and human populations. Such a compound might also be used to treat blood products prior to transfusion. PS-ON study might also help scientists better understand how normal proteins transform into abnormal, harmful forms. Further study is planned using PS-ONs in other types of TSEs aside from scrapie.
Information about this work, led by David Kocisko, Ph.D., and Byron Caughey, Ph.D., of RML is available in the March 2006 edition of Antimicrobial Agents and Chemotherapy.
Reference
Kocisko, D. et al. Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides. Antimicrobial Agents and Chemotherapy, March 2006, p. 1034-1044, Vol. 50, No. 3. DOI: 10.1128/AAC.50.3.1034-1044.2006
back to top