| Literature DB >> 17872544 |
Yuichi Murayama1, Miyako Yoshioka, Hiroyuki Okada, Masuhiro Takata, Takashi Yokoyama, Shirou Mohri.
Abstract
Prions, infectious agents causing transmissible spongiform encephalopathy (TSE), are composed primarily of the pathogenic form (PrP(Sc)) of the host-encoded prion protein. Although very low levels of infectivity have been detected in urine from scrapie-infected rodents, no reports of urinary PrP(Sc) have been substantiated. Studies on the dynamics of urinary PrP(Sc) during infection are needed to ensure the safety of urine-derived biopharmaceuticals and to assess the possible horizontal transmission of prion diseases. Using the protein misfolding cyclic amplification technique, a time-course study of urinary excretion and blood levels of PrP(Sc) was performed in Sc237-infected hamsters and a high rate of PrP(Sc) excretion was found during the terminal stage of the disease. Following oral administration, PrP(Sc) was present in all buffy coat samples examined; it was also present in most of the plasma samples obtained from hamsters in the symptomatic stage. PrP(Sc) was excreted in urine for a few days after oral administration; subsequently, urinary PrP(Sc) was not detected until the terminal disease stage. These results represent the first biochemical detection of PrP(Sc) in urine from TSE-infected animals.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17872544 DOI: 10.1099/vir.0.82786-0
Source DB: PubMed Journal: J Gen Virol ISSN: 0022-1317 Impact factor: 3.891