NR ALIV
AU Takahashi,H.; Takahashi,R.H.; Hasegawa,H.; Horiuchi,M.; Shinagawa,M.; Yokoyama,T.; Kimura,K.; Haritani,M.; Kurata,T.; Nagashima,K.
TI Characterization of antibodies raised against bovine-PrP-peptides
QU Journal of Neurovirology 1999 Jun; 5(3): 300-7
PT journal article
AB To analyze the antigenicity of peptides derived from bovine prion protein (PrP) cDNA, we immunized rabbits with four synthetic peptides and compared the immunoreactivity of antibodies to PrPs from various species by immunoblotting and immunohistochemistry. Two of the antibodies reacted strongly with all PrPs. The other antibodies, raised against overlapping peptides close to two glycosylation sites, did not recognize PrPsc-mouse but did recognize PrPsc-sheep which contains two sugar residues and PrPcJD with or without a sugar residue. Our results suggest that these antibodies may have species-specificity for both glycosylation status and amino acid sequences of the protein. In conclusion, we identified two regions in bovine-PrP which appear suitable for raising antibodies that detect various kinds of PrPs, and one region (Ab103-121) which appears suitable for raising antibodies that detect several species of PrPs. These antibodies may be useful for diagnosing prion diseases and for researching their pathogenesis.
MH Amino Acid Sequence; Animal; Antibody Specificity; Blotting, Western; Brain/metabolism; Cattle; Cerebellum/metabolism; Comparative Study; Creutzfeldt-Jakob Syndrome/metabolism; Encephalopathy, Bovine Spongiform/metabolism; Epitopes/metabolism; Human; Immunohistochemistry; Mice; Molecular Sequence Data; Peptides/genetics/*immunology; Prions/genetics/*immunology; Rabbits; Sequence Alignment; Sheep; Species Specificity; Support, Non-U.S. Gov't
AD Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
SP englisch
PO England