Detection of species specific epitopes of mouse and hamster prion proteins (PrPs) by anti-peptide antibodies.
Antisera to four synthetic peptides containing the substitutions between mouse and hamster prion proteins (PrPs) were produced in rabbits. The synthetic peptides used represent two mouse (Mo-I: residues 100-115 and Mo-V: residues 199-208) and two hamster PrP subregion sequences (Ha-I: 101-116 and Ha-V: 200-209). All antisera reacted strongly with homologous peptides but either not at all or poorly with heterologous peptides in enzymelinked immunosorbent assay (ELISA). Antisera to Mo-I and Mo-V recognized mouse PrPSc but not hamster PrpSc in western blot analysis (WB) and ELISA. Antisera to Ha-I contain antibodies specific to hamster PrPSc. The results indicate that these regions of PrPSc constitute species-specific epitopes. In contrast to these antisera, the antiserum to Ha-V recognized neither hamster nor mouse PrPSc. In this study, we identified mouse subregion-V as a species-specific epitope.
Yokoyama
T
T
National Institute of Animal Health, Ibaraki, Japan.
Itohara
S
S
Yuasa
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D000918:Antibody Specificity; D006224:Cricetinae; D000939:Epitopes / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011328:Prions / Q000138:chemical synthesis / Q000276:immunology*; D011817:Rabbits; D013045:Species Specificity
D000906:Antibodies; D000939:Epitopes; D010455:Peptides; D011328:Prions