Literature DB >> 8270103

Foreign PrP expression and scrapie infection in tissue culture cell lines.

B Chesebro1, K Wehrly, B Caughey, J Nishio, D Ernst, R Race.   

Abstract

PrP expression and scrapie infectivity was studied in a group of tissue culture cell lines from mice, hamsters, rats and humans. Cell surface PrP protein was detected in seven of ten cell lines from a variety of tissues and showed both cell surface and cytoplasmic perinuclear distributions. Mouse N2a neuroblastoma cells could be persistently infected with scrapie in vitro, but OBL-21 mouse neuroma cells were never successfully infected. Foreign PrP molecules including hamster PrP, mutant hamster PrP with leucine at amino acid 102, and mutant mouse PrP expressing a hamster-encoded PrP antigen epitope were expressed in mouse N2a cells. However, none of these cell lines could be successfully infected with the 263K hamster scrapie agent. Furthermore, expression of these foreign PrP molecules did not lead to spontaneous generation of protease-resistant PrP or a transmissible scrapie-like agent in vitro.

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Year:  1993        PMID: 8270103

Source DB:  PubMed          Journal:  Dev Biol Stand        ISSN: 0301-5149


  14 in total

1.  Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems. An update.

Authors:  B Caughey; G J Raymond; S A Priola; D A Kocisko; R E Race; R A Bessen; P T Lansbury; B Chesebro
Journal:  Mol Biotechnol       Date:  1999-11       Impact factor: 2.695

2.  Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.

Authors:  S A Priola; J Chabry; K Chan
Journal:  J Virol       Date:  2001-05       Impact factor: 5.103

3.  Near-infrared fluorescence imaging of apoptotic neuronal cell death in a live animal model of prion disease.

Authors:  Victoria A Lawson; Cathryn L Haigh; Blaine Roberts; Vijaya B Kenche; Helen M J Klemm; Colin L Masters; Steven J Collins; Kevin J Barnham; Simon C Drew
Journal:  ACS Chem Neurosci       Date:  2010-09-30       Impact factor: 4.418

4.  Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein.

Authors:  N Nishida; D A Harris; D Vilette; H Laude; Y Frobert; J Grassi; D Casanova; O Milhavet; S Lehmann
Journal:  J Virol       Date:  2000-01       Impact factor: 5.103

5.  Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation.

Authors:  Roger A Moore; Christian Herzog; John Errett; David A Kocisko; Kevin M Arnold; Stanley F Hayes; Suzette A Priola
Journal:  Protein Sci       Date:  2006-02-01       Impact factor: 6.725

6.  A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner.

Authors:  Young Pyo Choi; Suzette A Priola
Journal:  J Virol       Date:  2013-08-21       Impact factor: 5.103

7.  Effect of divalent metals on the neuronal proteasomal system, prion protein ubiquitination and aggregation.

Authors:  A G Kanthasamy; C Choi; H Jin; D S Harischandra; V Anantharam; A Kanthasamy
Journal:  Toxicol Lett       Date:  2012-09-17       Impact factor: 4.372

8.  Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.

Authors:  I Vorberg; K Chan; S A Priola
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

9.  Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells.

Authors:  S A Priola; B Caughey; R E Race; B Chesebro
Journal:  J Virol       Date:  1994-08       Impact factor: 5.103

10.  Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier.

Authors:  D A Kocisko; S A Priola; G J Raymond; B Chesebro; P T Lansbury; B Caughey
Journal:  Proc Natl Acad Sci U S A       Date:  1995-04-25       Impact factor: 11.205

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