ERA

Download the full-sized PDF of The POM monoclonals: A comprehensive set of antibodies to non-overlapping prion protein epitopesDownload the full-sized PDF

Analytics

Share

Permanent link (DOI): https://doi.org/10.7939/R3ZK56094

Download

Export to: EndNote  |  Zotero  |  Mendeley

Communities

This file is in the following communities:

Agricultural, Food and Nutritional Science, Department of

Collections

This file is in the following collections:

Journal Articles (Agricultural, Food and Nutritional Science)

The POM monoclonals: A comprehensive set of antibodies to non-overlapping prion protein epitopes Open Access

Descriptions

Author or creator
Polymenidou, Magdalini
Moos, Rita
Scott, Mike
Sigurdson, Christina
Shi, Yong-zhong
Yajima, Bill
Hafner-Bratkovič, Iva
Jerala, Roman
Hornemann, Simone
Wuthrich, Kurt
Bellon, Anne
Vey, Martin
Garen, Graciela
James, Michael N. G.
Kav, Nat
Aguzzi, Adriano
Additional contributors
Subject/Keyword
Peptide Mapping
Antibodies
Immunohistochemistry Techniques
Flow Cytometry
Recombinant Proteins
Cloning
Enzyme-Linked Immunoassays
Immunoprecipitation
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
PrPSc, a misfolded and aggregated form of the cellular prion protein PrPC, is the only defined constituent of the transmissible agent causing prion diseases. Expression of PrPC in the host organism is necessary for prion replication and for prion neurotoxicity. Understanding prion diseases necessitates detailed structural insights into PrPC and PrPSc. Towards this goal, we have developed a comprehensive collection of monoclonal antibodies denoted POM1 to POM19 and directed against many different epitopes of mouse PrPC. Three epitopes are located within the N-terminal octarepeat region, one is situated within the central unstructured region, and four epitopes are discontinuous within the globular C-proximal domain of PrPC. Some of these antibodies recognize epitopes that are resilient to protease digestion in PrPSc. Other antibodies immunoprecipitate PrPC, but not PrPSc. A third group was found to immunoprecipitate both PrP isoforms. Some of the latter antibodies could be blocked with epitope-mimicking peptides, and incubation with an excess of these peptides allowed for immunochromatography of PrPC and PrPSc. Amino-proximal antibodies were found to react with repetitive PrPC epitopes, thereby vastly increasing their avidity. We have also created functional single-chain miniantibodies from selected POMs, which retained the binding characteristics despite their low molecular mass. The POM collection, thus, represents a unique set of reagents allowing for studies with a variety of techniques, including western blotting, ELISA, immunoprecipitation, conformation-dependent immunoassays, and plasmon surface plasmon resonance-based assays.
Date created
2008
DOI
doi:10.7939/R3ZK56094
License information

Rights
Attribution 4.0 International
Citation for previous publication
Polymenidou, M., Moos, R., Scott, M., Sigurdson, C., Shi, Y. -Z., Yajima, W., Hafner-Bratkovič, I., Jerala, R., Hornemann, S., Wuthrich, K., Bellon, A., Vey, M., Garen, G., James, M. N. G., Kav, N., & Aguzzi, A. (2008). The POM monoclonals: A comprehensive set of antibodies to non-overlapping prion protein epitopes. PLoS ONE, 3(12), e3872 [17 pages].  http://dx.doi.org/10.1371/journal.pone.0003872

Source

Link to related item

File Details

Date Uploaded
Date Modified
Audit Status
Audits have not yet been run on this file.
Characterization
File format: pdf (PDF/A)
Mime type: application/pdf
File size: 689451
Last modified: 2017:09:06 16:38:07-06:00
Filename: PLoSONE_3_12_e3872.PDF
Original checksum: a78c128685e1d0b8b221c71c18923f97
Well formed: true
Valid: true
File title: pone.0003872 1..17
Page count: 17
Activity of users you follow
User Activity Date