Antigenic profile of human recombinant PrP: generation and chracterization of a versatile polyclonal antiserum

M. Sachsamanoglou; I. Paspaltzis; S. Petrakis; S. Verghese-Nikolakaki; C.H. Panagiotidis; T. Voitlander; H. Budka; J.P.M. Langeveld; T. Sklaviadis

doi:10.1016/j.jneuroim.2003.09.018

Antigenic profile of human recombinant PrP: generation and chracterization of a versatile polyclonal antiserum

M. Sachsamanoglou, I. Paspaltzis, S. Petrakis, S. Verghese-Nikolakaki, C.H. Panagiotidis, T. Voitlander, H. Budka, J.P.M. Langeveld, T. Sklaviadis

Research output: Contribution to journal › Article › Academic › peer-review

13 Citations (Scopus)

Abstract

We describe the quality of a rabbit polyclonal antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.

Original language	English
Pages (from-to)	22-32
Journal	Journal of Neuroimmunology
Volume	146
Issue number	1
DOIs	https://doi.org/10.1016/j.jneuroim.2003.09.018
Publication status	Published - 2004

Keywords

bovine spongiform encephalopathy
creutzfeldt-jakob-disease
scrapie prion proteins
monoclonal-antibodies
peptide
sheep
mice
gene
immunoreactivity
surveillance

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.jneuroim.2003.09.018

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Sachsamanoglou, M., Paspaltzis, I., Petrakis, S., Verghese-Nikolakaki, S., Panagiotidis, C. H., Voitlander, T., Budka, H., Langeveld, J. P. M., & Sklaviadis, T. (2004). Antigenic profile of human recombinant PrP: generation and chracterization of a versatile polyclonal antiserum. Journal of Neuroimmunology, 146(1), 22-32. https://doi.org/10.1016/j.jneuroim.2003.09.018

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abstract = "We describe the quality of a rabbit polyclonal antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.",

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author = "M. Sachsamanoglou and I. Paspaltzis and S. Petrakis and S. Verghese-Nikolakaki and C.H. Panagiotidis and T. Voitlander and H. Budka and J.P.M. Langeveld and T. Sklaviadis",

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AU - Sachsamanoglou, M.

AU - Paspaltzis, I.

AU - Petrakis, S.

AU - Verghese-Nikolakaki, S.

AU - Panagiotidis, C.H.

AU - Voitlander, T.

AU - Budka, H.

AU - Langeveld, J.P.M.

AU - Sklaviadis, T.

PY - 2004

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N2 - We describe the quality of a rabbit polyclonal antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.

AB - We describe the quality of a rabbit polyclonal antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.

KW - bovine spongiform encephalopathy

KW - creutzfeldt-jakob-disease

KW - scrapie prion proteins

KW - monoclonal-antibodies

KW - peptide

KW - sheep

KW - mice

KW - gene

KW - immunoreactivity

KW - surveillance

U2 - 10.1016/j.jneuroim.2003.09.018

DO - 10.1016/j.jneuroim.2003.09.018

M3 - Article

SN - 0165-5728

VL - 146

SP - 22

EP - 32

JO - Journal of Neuroimmunology

JF - Journal of Neuroimmunology

IS - 1

ER -

Antigenic profile of human recombinant PrP: generation and chracterization of a versatile polyclonal antiserum

Abstract

Keywords

UN SDGs

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