Prion protein expression in different species: Analysis with a panel of new mAbs
- 21 July 1998
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 95 (15) , 8812-8816
- https://doi.org/10.1073/pnas.95.15.8812
Abstract
By immunizing prion knockout mice ( Prnp −/−) with recombinant murine prion protein (PrP c ), we obtained a panel of mAbs specific for murine PrP c . These mAbs can be applied to immunoblotting, cell surface immunofluorescent staining, and immunohistochemistry at light and electron microscopy. These mAbs recognize both the normal (PrP c ) and protease-resistant (PrP res ) isoforms of PrP. Some mAbs are species restricted, while others react with PrP from a broad range of mammals including mice, humans, monkeys, cows, sheep, squirrels, and hamsters. Moreover, some of the mAbs selectively recognize different PrP glycoforms as well as the metabolic fragments of PrP c . These newly generated PrP c antibodies will help to explore the biology of PrP c and to establish the diagnosis of prion diseases in both humans and animals.Keywords
This publication has 31 references indexed in Scilit:
- Effect of the D178N Mutation and the Codon 129 Polymorphism on the Metabolism of the Prion ProteinPublished by Elsevier ,1996
- A new variant of Creutzfeldt-Jakob disease in the UKPublished by Elsevier ,1996
- Normal host prion protein necessary for scrapie-induced neurotoxicityNature, 1996
- Truncated Forms of the Human Prion Protein in Normal Brain and in Prion DiseasesJournal of Biological Chemistry, 1995
- Regional distribution of protease‐resistant prion protein in fatal familial insomniaAnnals of Neurology, 1995
- Prion Protein Gene Variation Among PrimatesJournal of Molecular Biology, 1995
- Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells.The Journal of cell biology, 1990
- Scrapie prions aggregate to form amyloid-like birefringent rodsCell, 1983
- Further purification and characterization of scrapie prionsBiochemistry, 1982
- Novel Proteinaceous Infectious Particles Cause ScrapieScience, 1982