Abstract |
Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity when challenged with PrP from diverse species. We have produced an antibody [monoclonal antibody (mAb) 2-40] raised against a synthetic peptide corresponding to residues (106-126 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (i.e., sheep, hamsters, and mice). Together with the fact that it recognizes the whole PrP in both cellular and scrapie isoforms, mAb 2-40 may be helpful in studying conformational changes of the PrP, as well as establishing a possible connection between human and animal diseases.
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Authors | E Hanan, S A Priola, B Solomon |
Journal | Cellular and molecular neurobiology
(Cell Mol Neurobiol)
Vol. 21
Issue 6
Pg. 693-703
(Dec 2001)
ISSN: 0272-4340 [Print] United States |
PMID | 12043842
(Publication Type: Journal Article)
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Chemical References |
- Amyloid
- Antibodies, Monoclonal
- Epitopes
- Peptide Fragments
- PrPC Proteins
- PrPSc Proteins
- Protein Isoforms
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Topics |
- Amyloid
(chemistry)
- Animals
- Antibodies, Monoclonal
(immunology, isolation & purification)
- Blotting, Western
- Cricetinae
- Epitope Mapping
- Epitopes
(immunology)
- Gene Library
- Humans
- Immunohistochemistry
- Peptide Fragments
(chemical synthesis, immunology)
- PrPC Proteins
(immunology, metabolism)
- PrPSc Proteins
(immunology, metabolism)
- Prion Diseases
(diagnosis, immunology, physiopathology)
- Protein Binding
(immunology)
- Protein Isoforms
(immunology, metabolism)
- Sequence Homology, Amino Acid
- Sheep
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