NR ABAF
AU Baron,T.G.M.; Betemps,D.; Groschup,M.H.; Madec,J.Y.
TI Immunological characterization of the sheep prion protein expressed as fusion proteins in Escherichia coli
QU FEMS Immunology and Medical Microbiology 1999 Sep; 25(4): 379-84
PT journal article
AB The prion protein (PrP) from sheep was produced in large quantities of entire protein in Escherichia coli after fusion with a carboxy-terminal hexahistidine sequence. In contrast, amino-terminal fusion with glutathione S-transferase (GST) revealed a high susceptibility toward cleavage of the protein. Both recombinant proteins were recognised, at variable levels, in Western blots using a panel of antibodies against the 40-56, 89-104, 98-113 and 112-115 sequences of the prion protein, similarly to the abnormal prion protein extracted from scrapie-infected sheep. Interestingly, monoclonal antibody 3F4 was found to react with these three proteins in Western blot.
MH Animal; Cloning, Molecular; Escherichia coli; Gene Expression; Glutathione Transferase/genetics/metabolism; Histidine; Prions/genetics/*immunology/metabolism; Recombinant Fusion Proteins/genetics/immunology/metabolism; Sheep; Support, Non-U.S. Gov't
AD Agence Francaise de Securite Sanitaire des Aliments, Lyon, France. t.baron@lyon.afssa.fr
SP englisch
PO Niederlande