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

• Published in: Journal of virological methods 2006-05, Vol.133 (2), p.205-210
• Main Authors: Halimi, Michele, Dayan-Amouyal, Yael, Kariv-Inbal, Zehavit, Friedman-Levi, Yael, Mayer-Sonnenfeld, Tehila, Gabizon, Ruth
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Carrier Proteins - drug effects; Carrier Proteins - urine; Case-Control Studies; CJD; Coloring Agents - pharmacology; Congo red; Congo Red - pharmacology; Creutzfeldt-Jakob Syndrome - urine; Fundamental and applied biological sciences. Psychology; Glycosaminoglycans; Glycosaminoglycans - urine; Humans; Light chain IgG; Microbiology; Prion; Prions - chemistry; Prions - urine; Protein Binding - drug effects; Specimen Handling; Techniques used in virology; Urine; Virology
• ISSN: 0166-0934; 1879-0984
• DOI: 10.1016/j.jviromet.2005.11.011

Light chain IgG, a known amyloidotic protein, is present in the urine of prion disease affected individuals in a protease resistant form. In addition, it was shown recently that prion urine samples comprise a significant excess of glycosaminoglycans. Since amyloidotic proteins and glycosaminoglycans are the major components of amyloid aggregates, a Congo red dot blot assay was developed for detection of Creutzfeldt–Jacob disease (CJD) in urine. This assay was also positive for about 10% of patients suffering from diseases such as Alzheimer disease, cerebrovascular attacks and multiple sclerosis, but negative for healthy controls. Both glycosaminoglycans and proteins such as light chain IgG were required for the binding of Congo red to the urine fractions, as shown by the fact that Proteinase K digestion of the samples either after guanidine or after choindrotinase abolished the Congo red signal from the CJD samples.