Literature DB >> 6431296

Antibodies to a scrapie prion protein.

P E Bendheim, R A Barry, S J DeArmond, D P Stites, S B Prusiner.   

Abstract

Scrapie is a slow infection of the nervous system which progresses in the absence of any apparent immune response. The recent development of a large-scale purification protocol for scrapie prions made it possible to obtain substantial quantities of electrophoretically purified prion protein (PrP 27-30) and we report here on the successful production of a rabbit antiserum to PrP 27-30. The antiserum reacted with PrP 27-30 and several lower molecular weight proteins as shown by Western blots; it did not react with protein preparations from uninfected brains. Discrete structures in the subependymal region of scrapie-infected hamster brains were stained immunocytochemically. These same structures also stained with Congo red dye and showed green birefringence with polarized light, a characteristic of purified prion rods. This staining pattern suggests that they are amyloid plaques.

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Year:  1984        PMID: 6431296     DOI: 10.1038/310418a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  66 in total

1.  Conformation-dependent high-affinity monoclonal antibodies to prion proteins.

Authors:  Larry H Stanker; Ana V Serban; Elisa Cleveland; Robert Hnasko; Azucena Lemus; Jiri Safar; Stephen J DeArmond; Stanley B Prusiner
Journal:  J Immunol       Date:  2010-06-07       Impact factor: 5.422

2.  Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.

Authors:  M Gasset; M A Baldwin; D H Lloyd; J M Gabriel; D M Holtzman; F Cohen; R Fletterick; S B Prusiner
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-15       Impact factor: 11.205

3.  Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein.

Authors:  R A Williamson; D Peretz; N Smorodinsky; R Bastidas; H Serban; I Mehlhorn; S J DeArmond; S B Prusiner; D R Burton
Journal:  Proc Natl Acad Sci U S A       Date:  1996-07-09       Impact factor: 11.205

4.  N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state.

Authors:  B Caughey; G J Raymond; D Ernst; R E Race
Journal:  J Virol       Date:  1991-12       Impact factor: 5.103

5.  Scrapie-associated prion protein accumulates in astrocytes during scrapie infection.

Authors:  J F Diedrich; P E Bendheim; Y S Kim; R I Carp; A T Haase
Journal:  Proc Natl Acad Sci U S A       Date:  1991-01-15       Impact factor: 11.205

6.  Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis.

Authors:  M P McKinley; R K Meyer; L Kenaga; F Rahbar; R Cotter; A Serban; S B Prusiner
Journal:  J Virol       Date:  1991-03       Impact factor: 5.103

7.  Protease sensitivity and nuclease resistance of the scrapie agent propagated in vitro in neuroblastoma cells.

Authors:  K Neary; B Caughey; D Ernst; R E Race; B Chesebro
Journal:  J Virol       Date:  1991-02       Impact factor: 5.103

8.  Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes.

Authors:  J F Diedrich; H Minnigan; R I Carp; J N Whitaker; R Race; W Frey; A T Haase
Journal:  J Virol       Date:  1991-09       Impact factor: 5.103

9.  A new method to classify amyloid fibril proteins.

Authors:  T Kitamoto; J Tateishi; K Hikita; H Nagara; I Takeshita
Journal:  Acta Neuropathol       Date:  1985       Impact factor: 17.088

Review 10.  Protein-glycosaminoglycan interactions: infectiological aspects.

Authors:  D Sawitzky
Journal:  Med Microbiol Immunol       Date:  1996-02       Impact factor: 3.402

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