1998
DOI: 10.1128/jvi.72.11.9413-9418.1998
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Mapping the Prion Protein Using Recombinant Antibodies

Abstract: The fundamental event in prion disease is thought to be the posttranslational conversion of the cellular prion protein (PrPC) into a pathogenic isoform (PrPSc). The occurrence of PrPC on the cell surface and PrPSc in amyloid plaques in situ or in aggregates following purification complicates the study of the molecular events that underlie the disease process. Monoclonal antibodies are highly sensitive probes of protein conformation which can be used under these conditions. Here, we report the rescue of a diver… Show more

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Cited by 203 publications
(92 citation statements)
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“…However, we found one clear difference, which is that mAb T2 required the C-terminal residues 212-217 to react intensely with recombinant MoPrP peptides (Table 1), and this result indicates that the C-terminal residues 212-217 constitute a part of the discontinuous epitope of mAb T2 or are required indirectly to structure the mAb T2 epitope. Moreover, the heavy chain CDR3 sequence of mAb T2 from phage antibody clone 2-2, 'SDLWFAY' (Y. Tagawa, unpublished data), differs from the CDR3 sequence of Fab D18 'FYYGMDY' (25). Therefore, we conclude that mAb T2 is a novel mAb that recognizes a discontinuous epitope which we presume to be structured within residues 132-217.…”
Section: Discussionmentioning
confidence: 80%
“…However, we found one clear difference, which is that mAb T2 required the C-terminal residues 212-217 to react intensely with recombinant MoPrP peptides (Table 1), and this result indicates that the C-terminal residues 212-217 constitute a part of the discontinuous epitope of mAb T2 or are required indirectly to structure the mAb T2 epitope. Moreover, the heavy chain CDR3 sequence of mAb T2 from phage antibody clone 2-2, 'SDLWFAY' (Y. Tagawa, unpublished data), differs from the CDR3 sequence of Fab D18 'FYYGMDY' (25). Therefore, we conclude that mAb T2 is a novel mAb that recognizes a discontinuous epitope which we presume to be structured within residues 132-217.…”
Section: Discussionmentioning
confidence: 80%
“…The key feature of prion disease is the conversion, involving a conformational change, of PrP c to PrP sc : several regions of PrP have been shown to be involved in this process. 11,[25][26][27] One such region, including residues 90-141 of the PrP (PrP90-141), is considered to be functionally important for Figure 2 Immunoblotting of brain homogenates from Creutzfeldt-Jakob disease (CJD)-infected human (H) and mouse model (M) with anti-PrP mAbs 2E7, 2D10, 6G4, 7C1, 8A4, 4D6, 6F4, 8E7, 5G7 and a control anti-PrP (3F4). The brain materials were treated with proteinase K (+) or left untreated (-) as indicated.…”
Section: Discussionmentioning
confidence: 99%
“…We found 3 known epitopes for the unbound ovine prion between residues 121 and 230: residues 132-156, 21,22 163-171, 23 and 220 -231. 22 Thus, we performed 4 rounds of docking sampling: CDRs versus epitope I, CDRs versus epitope II, CDRs versus epitope III, and CDRs versus the entire surface of prion.…”
Section: Target 19 (Unbound Ovine Prion-bound Antibody)mentioning
confidence: 88%