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Literature DB >> 7494285

A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells.

Abstract

Neurodegeneration caused by the transmissible spongiform encephalopathies is associated with the conversion of a normal host protein, PrP-sen, into an abnormal aggregated protease-resistant form, PrP-res. In scrapie-infected mouse neuroblastoma cells, mouse PrP-sen is converted into PrP-res but recombinant hamster PrP-sen expressed in these cells is not. In the present studies, recombinant hamster/mouse PrP-sen molecules were expressed in these scrapie-infected cells to define specific PrP amino acid residues critical for the conversion to PrP-res. The results showed that homology to the region of mouse PrP-sen from amino acid residues 112 to 138 was required for conversion of recombinant PrP-sen to PrP-res in scrapie-infected mouse cells. Furthermore, a single hamster-specific PrP amino acid at residue 138 could inhibit the conversion of the recombinant PrP-sen into PrP-res. The data are consistent with studies in humans which show that specific amino acid residue changes within PrP can influence disease pathogenesis and transmission of transmissible spongiform encephalopathies across species barriers.

Entities: Disease Gene Species

Mesh：

Substances：

Year: 1995 PMID： 7494285 PMCID： PMC189717

Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103

39 in total

1. Self-replication and scrapie.

Authors: J S Griffith
Journal: Nature Date: 1967-09-02 Impact factor: 49.962

2. A kinetic model for amyloid formation in the prion diseases: importance of seeding.

Authors: J H Come; P E Fraser; P T Lansbury
Journal: Proc Natl Acad Sci U S A Date: 1993-07-01 Impact factor: 11.205

3. An amber mutation of prion protein in Gerstmann-Sträussler syndrome with mutant PrP plaques.

Authors: T Kitamoto; R Iizuka; J Tateishi
Journal: Biochem Biophys Res Commun Date: 1993-04-30 Impact factor: 3.575

4. Mice devoid of PrP are resistant to scrapie.

Authors: H Büeler; A Aguzzi; A Sailer; R A Greiner; P Autenried; M Aguet; C Weissmann
Journal: Cell Date: 1993-07-02 Impact factor: 41.582

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

Authors: B Chesebro; K Wehrly; B Caughey; J Nishio; D Ernst; R Race
Journal: Dev Biol Stand Date: 1993

6. Chimeric prion protein expression in cultured cells and transgenic mice.

Authors: M R Scott; R Köhler; D Foster; S B Prusiner
Journal: Protein Sci Date: 1992-08 Impact factor: 6.725

7. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes.

Authors: M Scott; D Groth; D Foster; M Torchia; S L Yang; S J DeArmond; S B Prusiner
Journal: Cell Date: 1993-06-04 Impact factor: 41.582

8. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism.

Authors: L G Goldfarb; R B Petersen; M Tabaton; P Brown; A C LeBlanc; P Montagna; P Cortelli; J Julien; C Vital; W W Pendelbury
Journal: Science Date: 1992-10-30 Impact factor: 47.728

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. Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells.

Authors: B Caughey; G J Raymond
Journal: J Virol Date: 1993-02 Impact factor: 5.103

52 in total

1. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.

Authors: C Wong; L W Xiong; M Horiuchi; L Raymond; K Wehrly; B Chesebro; B Caughey
Journal: EMBO J Date: 2001-02-01 Impact factor: 11.598

2. Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence.

Authors: J Chabry; S A Priola; K Wehrly; J Nishio; J Hope; B Chesebro
Journal: J Virol Date: 1999-08 Impact factor: 5.103

3. Glycosylation influences cross-species formation of protease-resistant prion protein.

Authors: S A Priola; V A Lawson
Journal: EMBO J Date: 2001-12-03 Impact factor: 11.598

4. 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

5. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.

Authors: Bishwajit Kundu; Nilesh R Maiti; Eric M Jones; Krystyna A Surewicz; David L Vanik; Witold K Surewicz
Journal: Proc Natl Acad Sci U S A Date: 2003-09-30 Impact factor: 11.205

6. Structure of the β2-α2 loop and interspecies prion transmission.

Authors: Cyrus Bett; Natalia Fernández-Borges; Timothy D Kurt; Melanie Lucero; K Peter R Nilsson; Joaquín Castilla; Christina J Sigurdson
Journal: FASEB J Date: 2012-04-09 Impact factor: 5.191

7. Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie.

Authors: A J Raeber; R E Race; S Brandner; S A Priola; A Sailer; R A Bessen; L Mucke; J Manson; A Aguzzi; M B Oldstone; C Weissmann; B Chesebro
Journal: EMBO J Date: 1997-10-15 Impact factor: 11.598