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Published online ahead of print on 17 February 2009 as doi:10.1099/vir.2008.007120-0
Journal of General Virology 2009;90:1048.

A more recent version of this article appeared on April 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.2008.007120-0
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Detection of typical and atypical BSE and scrapie prion strains by prion protein motif-grafted antibodies

Francesca Martucci1, Pierluigi Acutis1, Maria Mazza1, Sabrina Nodari1, Silvia Colussi1, Cristiano Corona1, Simone Barocci2, Armando Gabrielli3, Maria Caramelli1, Cristina Casalone1 and Gianluca Moroncini3,4

1 CEA, Italian Reference Laboratory for TSEs, Istituto Zooprofilattico Sperimentale del Piemonte;
2 Istituto Zooprofilattico Sperimentale dell'Umbria e delle Marche;
3 Clinica Medica, Dipartimento Scienze Mediche e Chirurgiche, Università Politecnica delle Marc

4 E-mail: g.moroncini{at}univpm.it

To further evaluate the reactivity of prion-specific monoclonal antibodies containing the 89-112 or the 136-158 prion protein (PrP) polypeptides, immunoprecipitations were performed on brain extracts from Italian bovines, sheep and goats with transmissible spongiform encephalopathies. No binding of IgG 89-112 or IgG 136-158 to PrP in normal brain extracts was detected. Conversely, both reagents immunoprecipitated PrP from bovine (BSE) and bovine amyloidotic (BASE) spongiform encephalopaties, and from typical and atypical scrapie brain extracts. The immunoprecipitated PrP bands mirrored the Western Blot (WB) profile of the different prion strains, indicating universal affinity of two independent PrP regions for disease-associated PrP conformers regardless of species source and strain properties. Immunoprecipitation with the motif-grafted antibodies increased sensitivity of conventional detection methods based on centrifugation followed by WB, as confirmed at assay of diluted samples with both methods. These reagents or derivative molecules may thus find broad application in prion diagnosis and research.

Received 8 September 2008; accepted 1 December 2008.




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