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Comparison of three monoclonal antibodies for use in immunohistochemical detection of bovine spongiform encephalopathy protease-resistant prion protein.

Salguero, FJ, Díaz-San, SF, Brun, A, Cano, MJ and Torres, JM (2006) Comparison of three monoclonal antibodies for use in immunohistochemical detection of bovine spongiform encephalopathy protease-resistant prion protein. J Vet Diagn Invest, 18 (1). pp. 106-109.

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Abstract

Confirmatory diagnosis of prion diseases in humans and animals relies on the histopathological examination and immunodetection of the protease-resistant isoform of prion protein (PrPres). The generation of novel PrP-specific monoclonal antibodies (MAbs) has greatly improved diagnostic methodology and basic research on prion diseases as well. In this study, the performance of 3 different PrP-specific MAbs in recognizing brain PrPres deposits from cows affected with bovine spongiform encephalopathy (BSE) was compared by using a standard immunohistochemical technique under different pretreatment conditions. All antibodies showed similar reactivity after denaturing treatment. However, greater differences were found among them after proteinase K treatment, even in the absence of a denaturing step. In fact, 1 MAb (2A11) was able to react with PrPres deposits in the absence of a denaturing step, yielding the strongest signal and confirming the usefulness of MAb 2A11 in immunohistochemistry for the diagnosis of BSE.

Item Type: Article
Authors :
NameEmailORCID
Salguero, FJUNSPECIFIEDUNSPECIFIED
Díaz-San, SFUNSPECIFIEDUNSPECIFIED
Brun, AUNSPECIFIEDUNSPECIFIED
Cano, MJUNSPECIFIEDUNSPECIFIED
Torres, JMUNSPECIFIEDUNSPECIFIED
Date : January 2006
Uncontrolled Keywords : Amino Acid Sequence, Animals, Antibodies, Monoclonal, Brain Stem, Cattle, Encephalopathy, Bovine Spongiform, Endopeptidase K, Epitopes, Immunohistochemistry, Molecular Sequence Data, Prions, Protein Denaturation
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:08
Last Modified : 17 May 2017 10:08
URI: http://epubs.surrey.ac.uk/id/eprint/826554

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