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Sensitive detection of aggregated prion protein via proximity ligation
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Science for Life Laboratory, SciLifeLab.
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2014 (English)In: Prion, ISSN 1933-6896, E-ISSN 1933-690X, Vol. 8, no 3, 261-265 p.Article in journal (Refereed) Published
Abstract [en]

The DNA assisted solid-phase proximity ligation assay (SP-PLA) provides a unique opportunity to specifically detect prion protein (PrP) aggregates by investigating the collocation of three or more copies of the specific protein. We have developed a SP-PLA that can detect PrP aggregates in brain homogenates from infected hamsters even after a 10(7)-fold dilution. In contrast, brain homogenate from uninfected animals did not generate a detectable signal at hundred-fold higher concentration. Using either of the two monoclonal anti-PrP antibodies 3F4 and 6H4 we successfully detected low concentrations of aggregated PrP. The presented results provide a proof of concept that this method might be an interesting tool in the development of diagnostic approaches of prion diseases.

Place, publisher, year, edition, pages
2014. Vol. 8, no 3, 261-265 p.
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Basic Medicine
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URN: urn:nbn:se:uu:diva-239529DOI: 10.4161/pri.32231ISI: 000348375500004PubMedID: 25482604OAI: oai:DiVA.org:uu-239529DiVA: diva2:774785
Available from: 2014-12-29 Created: 2014-12-29 Last updated: 2017-12-05Bibliographically approved

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Hammond, MariaWik, LottaLandegren, UlfKamali-Moghaddam, Masood

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Hammond, MariaWik, LottaLandegren, UlfKamali-Moghaddam, Masood
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Department of Immunology, Genetics and PathologyScience for Life Laboratory, SciLifeLab
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