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Volume 16, Number 1—January 2010

Letter

Distinct Molecular Signature of Bovine Spongiform Encephalopathy Prion in Pigs

Torsten SeuberlichComments to Author  and Andreas Zurbriggen
Author affiliations: University of Berne, Berne, Switzerland

Main Article

Figure

Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quant

Figure. Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quantity One software package (Bio-Rad, Rheinach, Switzerland). Data are based on 4 independent runs, and error bars indicate SD. Note the different extent of PrPres glycosylation in bovine and porcine BSE. By contrast, the molecular masses of the unglycosylated PrPres were similar and scored 18.89 kDa (SD ± 0.28 kDa) and 18.90 kDa (SD ± 0.42 kDa) in bovine and porcine BSE, respectively. Molecular masses of the standards are indicated on the left in panel A.

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