Prion urine comprises a glycosaminoglycan-light chain IgG complex that can be stained by Congo red

Halimi, Michele; Dayan-Amouyal, Yael; Kariv-Inbal, Zehavit; Friedman-Levi, Yael; Mayer-Sonnenfeld, Tehila; Gabizon, Ruth

doi:10.1016/j.jviromet.2005.11.011

Cited by 9 publications

(12 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This Ig was further characterized as PK-resistant IgG light chain fragments. In addition, Halimi et al (16) reported that urine from CJD patients comprises an amyloidotic aggregate of PK-resistant light chain IgG and glycosaminoglycans, mostly chondroitin sulfate. This PK-resistant property seems to be related to the presence of glycosaminoglycans in the urine of these patients, since digestion of the samples with choindroitinase rendered light chain IgG PK sensitive.…”

Section: Vol 85 2011mentioning

confidence: 99%

Prion Disease Detection, PMCA Kinetics, and IgG in Urine from Sheep Naturally/Experimentally Infected with Scrapie and Deer with Preclinical/Clinical Chronic Wasting Disease

Rubenstein

Chang

Gray

et al. 2011

J Virol

View full text Add to dashboard Cite

Section: Vol 85 2011mentioning

confidence: 99%

Prion Disease Detection, PMCA Kinetics, and IgG in Urine from Sheep Naturally/Experimentally Infected with Scrapie and Deer with Preclinical/Clinical Chronic Wasting Disease

Rubenstein

Chang

Gray

et al. 2011

J Virol

View full text Add to dashboard Cite

“…in a cellulose tubular membrane (pore range 6,000-8,000 dalton; FPI, Tex., USA) against 5 liters of saline at 4 ° C (saline was changed twice during dialysis). Subsequently, the urine samples were centrifuged at high speed (100,000 g for 1 h at 4 ° C) [16,18,19] . Pellets were resuspended in 1% BSA/PBS.…”

Section: In Vivo Experimentsmentioning

confidence: 99%

“…Following a first clearing centrifugation as described above, urine samples were concentrated by minicon B15 clinical sample concentrators (Millipore) [17,19] . Before enrichment, all urine samples were tested for creatinine concentrations by an automated procedure.…”

Section: Urine Studiesmentioning

confidence: 99%

Urine from Scrapie-Infected Hamsters Comprises Low Levels of Prion Infectivity

et al. 2006

Self Cite

View full text Add to dashboard Cite

The question of whether prion diseases can be transmitted by body fluids has important epidemiological, environmental and economical implications. In this work, we set to investigate whether urine collected from scrapie-infected hamsters can transmit fatal or subclinical infectivity to normal hamsters. After prolonged incubation times ranging from 300 to 700 days, a small number of animals inoculated with scrapie urine succumbed to scrapie disease, and several asymptomatic hamsters presented low levels of PrP^Sc in their brains. In addition, most of the asymptomatic hamsters inoculated with scrapie urine, as opposed to those inoculated with normal urine, presented extensive gliosis as well as protease-resistant light chain IgG in their urine, a molecule shown by us and others to be a surrogate marker for prion infection. Our results suggest that urine from scrapie-infected hamsters can transmit a widespread subclinical disease that in some cases develops into fatal scrapie.

show abstract

“…However, urine PrP Sc may have certain features different from those of brain PrP Sc , as injections with the former do not cause prion disease [119]. Recently, several laboratories have reported that urine-derived PrP Sc comprises immunoglobulins or bacterial outer membrane proteins [29,35,118]. On the other hand, others have reported that urinary proteins from scrapie-infected mice with lymphocytic nephritis induced scrapie upon inoculation into noninfected indicator mice [117].…”

Section: Urine Prp Scmentioning

confidence: 99%

“…In vitro conversion of the cellular isoform of prion protein (PrP C ) to form PrP Sc -like products has been demonstrated by incubating 35 S-labeled PrP C with PrP Sc . This produced a protease-resistant radioactive product with the mobility of protease-treated authentic PrP Sc [55].…”

mentioning

confidence: 99%

Recent Developments in Prion Disease Research: Diagnostic Tools and In Vitro Cell Culture Models

Sakudo

Nakamura

Ikuta

et al. 2007

The Journal of Veterinary Medical Science

View full text Add to dashboard Cite

ABSTRACT. After prion infection, an abnormal isoform of prion protein (PrP Sc ) converts the cellular isoform of prion protein (PrP C ) into PrP Sc . PrP C -to-PrP Sc conversion leads to PrP Sc accumulation and PrP C deficiency, contributing etiologically to induction of prion diseases. Presently, most of the diagnostic methods for prion diseases are dependent on PrP Sc detection. Highly sensitive/accurate specific detection of PrP Sc in many different samples is a prerequisite for attempts to develop reliable detection methods. Towards this goal, several methods have recently been developed to facilitate sensitive and precise detection of PrP Sc , namely, protein misfolding cyclic amplification, conformation-dependent immunoassay, dissociation-enhanced lanthanide fluorescent immunoassay, capillary gel electrophoresis, fluorescence correlation spectroscopy, flow microbead immunoassay, etc. Additionally, functionally relevant prion-susceptible cell culture models that recognize the complexity of the mechanisms of prion infection have also been pursued, not only in relation to diagnosis, but also in relation to prion biology. Prion protein (PrP) gene-deficient neuronal cell lines that can clearly elucidate PrP C functions would contribute to understanding of the prion infection mechanism. In this review, we describe the trend in recent development of diagnostic methods and cell culture models for prion diseases and their potential applications in prion biology. Evidence of prion infections has been established by the accumulation of an abnormal isoform of prion protein (PrP Sc ) and/or infectivity after multiple passages [54,85,94,131]. In vitro conversion of the cellular isoform of prion protein (PrP C ) to form PrP Sc -like products has been demonstrated by incubating 35 S-labeled PrP C with PrP Sc . This produced a protease-resistant radioactive product with the mobility of protease-treated authentic PrP Sc [55]. This in vitro conversion confirms the species-[90] and strain-specificities [7] observed in vivo. However, because the yield is less stoichiometric than for PrP Sc [55], it has not been possible to determine whether or not an increase in infectivity occurred [55]. Recent progress in the development of diagnostic methods for PrP Sc detection has dramatically facilitated many approaches in prion biology. The protein misfolding cyclic amplification (PMCA) method deserves special mention [96]. Hitherto, it has not been possible to renature completely denatured prion preparations to an infectious state [79,81]; however, the novel PMCA approach enables in vitro amplification of infectious prions [16].The susceptibility of cell lines, such as N2a, in an in vitro cell culture assay to prion infections has been assessed by exposing the cells to serial dilutions of prion-infected mouse brain homogenates, and the dilution rate yielding negative outcome in a blotting assay for PrP Sc has been determined to be the infectivity level. Prion concentrations equivalent to those determined in an animal bioassay [9] have ...

show abstract

Prion urine comprises a glycosaminoglycan-light chain IgG complex that can be stained by Congo red

Cited by 9 publications

References 25 publications

Prion Disease Detection, PMCA Kinetics, and IgG in Urine from Sheep Naturally/Experimentally Infected with Scrapie and Deer with Preclinical/Clinical Chronic Wasting Disease

Prion Disease Detection, PMCA Kinetics, and IgG in Urine from Sheep Naturally/Experimentally Infected with Scrapie and Deer with Preclinical/Clinical Chronic Wasting Disease

Urine from Scrapie-Infected Hamsters Comprises Low Levels of Prion Infectivity

Recent Developments in Prion Disease Research: Diagnostic Tools and In Vitro Cell Culture Models

Contact Info

Product

Resources

About