Julie Vergara

TL;DR: It is shown that antibodies binding cell-surface PrPC inhibit PrPSc formation in a dose-dependent manner, and this observations support the use of antibodies in the prevention and treatment of prion diseases and identify a region of PrPC for drug targeting.

TL;DR: The CDI is capable of measuring the disease-causing PrP isoform (PrPSc) in bovine brainstems with a sensitivity similar to that of end-point titrations in transgenic mice expressing BoPrP, and was able to discriminate between PrPSc from BSE-infected cattle and Tg(BoPrP) mice as well as from chronic wasting disease -infected deer and elk.

TL;DR: A causal relationship between species barriers, changes in PrP(Sc) conformation, and the emergence of new prion strains is suggested.

TL;DR: Although dominant-negative inhibition of wt PrPSc formation occurs, expression of the dominant- negative PrP at the same level as wtPrP does not prevent prion formation completely, and expression of dominant- Negative PrP alone had no deleterious effects on the mice and did not support prion propagation.

TL;DR: The 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.