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The complete mature bovine prion protein highly expressed in Escherichia coli: biochemical and structural studies
A Negro1, V De Filippis, S D Skaper
1Dipartimento di Chimica Biologica, Centro CNR dello Studio delle Biomembrane, Università di Padova, Padua, Italy.
Abstract:
According to the 'protein only' hypothesis, modification of the 3-dimensional fold of the constituent cellular protein, PrP(C), into the disease-associated isoform, PrP(Sc), is the cause of neurodegenerative diseases in animals and humans. Here we describe the high-level synthesis in Escherichia coli, and purification in the monomeric form, of a histidine-tagged full-length mature PrP (25-249) of bovine brain, termed His-PrP. Based on biochemical and spectroscopic data, His-PrP displays characteristics expected for the PrP(C) isoform. The reported expression system should allow the production of quantities of bovine PrP(C) sufficient to permit 3-dimensional structure determinations.