Cryptic epitopes in N-terminally truncated prion protein are exposed the full-length molecule: Dependence of conformation on pH

Proteins: Structure, Function and Genetics

Volumn 44, Issue 2, 2001, Pages 110-118

  Matsunaga, Yoichi ^a,b   Peretz, David ^a,b   Williamson, Anthony ^c   Burton, Dennis ^c   Mehlhorn, Ingrid ^a,b   Groth, Darlene ^a,b   Cohen, Fred E ^a,b   Prusiner, Stanley B ^a,b   Baldwin, Michael A ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Anti PrP antibodies; Circular dichroism; ELISA; Mass spectrometry; Prion disease; Recombinant prion protein

Indexed keywords

EPITOPE; GUANIDINE; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; PRION PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; COVALENT BOND; ENZYME LINKED IMMUNOSORBENT ASSAY; MASS SPECTROMETRY; MOUSE; NONHUMAN; PH; PRION DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN IMMOBILIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; ANTIGEN-ANTIBODY REACTIONS; CIRCULAR DICHROISM; CRICETINAE; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; GUANIDINE; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN FAB FRAGMENTS; MESOCRICETUS; MICE; MICE, KNOCKOUT; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PRIONS; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 0035427232     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1077     Document Type: Article

References (54)

1. Synthesis and trafficking of prion proteins in cultured cells
2. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform
3. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
4. Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system
5. Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein
6. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
7. Mapping the prion protein using recombinant antibodies
8. Sc)-specific epitope defined by a monoclonal antibody
9. Scrapie prions aggregate to form amyloid-like birefringent rods
10. A protease-resistant protein is a structural component of the scrapie prion
11. Molecular characteristics of the major scrapie prion protein
12. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells
13. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
14. Recombinant scrapie-like prion protein of 106 amino acids is soluble
15. Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice
16. NMR structure of the mouse prion protein domain PrP(121-231)
17. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
18. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
19. Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
20. Solution structure of Syrian hamster prion protein rPrP(90-231)
21. The cellular prion protein binds copper in vivo
22. Prion protein selectively binds copper (II) ions
23. Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
24. Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry
25. Pathologic conformations of prion proteins
26. Prion protein biology
27. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein
28. Physical studies of conformational plasticity in a recombinant prion protein
29. Purification and structural studies of a major scrapie prion protein
30. A cellular gene encodes scrapie PrP 27-30 protein
31. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
32. The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP)
33. Scrapie PrP 27-30 is a sialoglycoprotein
34. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
35. Scrapie prion protein contains a phosphatidylinositol glycolipid
36. Purification and properties of the cellular and scrapie hamster prion proteins
37. Cataloguing post-translational modifications of the scrapie prion protein by mass spectrometry
38. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
39. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
40. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
41. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
42. Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form
43. Proposed three-dimensional structure for the cellular prion protein
44. Scrapie prions: A three-dimensional model of an infectious fragment
45. Conformational transitions in peptides containing two putative α-helices of the prion protein
46. A transmembrane form of the prion protein in neurodegenerative disease
47. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
48. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
49. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
50. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
51. Structural clues to prion replication
52. Cell-free formation of protease-resistant prion protein
53. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform
54. Molecular properties of complexes formed between the prion protein and synthetic peptides