Avtor/Urednik		Čurin-Šerbec, Vladka; Bresjanac, Mara; Popović, Mara; Pretnar-Hartman, Katarina; Galvani, Vesna; Rupreht, Ruth; Černilec, Maja; Vranac, Tanja; Hafner, Iva; Jerala, Roman
Naslov		Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue
Tip		članek
Vir		J Biol Chem
Vol. in št.		Letnik 279, št. 5
Leto izdaje		2004
Obseg		str. 3694-8
Jezik		eng
Abstrakt		Current methods for diagnosing transmissible spongiform encephalopathies rely on the degradation of the cellular prion protein (PrPC) and the subsequent detection of the protease-resistant remnant of the pathological prion isoform PrPSc by antibodies that react with all forms of PrP. We report on a monoclonal antibody, V5B2, raised against a peptide from the C-terminal part of PrP, which recognizes an epitope specific to PrPgSc. In cryostat sections from Creutzfeldt-Jacob's disease (CJD) patients' brains, V5B2 selectively labels various deposits of PrPs without any pretreatment for removal of PrPC. V5B2 does not bind to non-CJD brain samples or to recombinant PrP, either in its native or denatured form. Specificity for PrP is confirmed by a sandwich enzyme-linked immunosorbent assay utilizing V5B2, which discriminates between CJD and normal samples without proteinase K treatment, and by immunoprecipitation from CJD brain homogenate. The PrPSc-specific epitope is disrupted by denaturation. We conclude that the C-terminal part of PrP in disease-associated PrPSc aggregates forms a structural epitope whose conformation is distinct from that of PrPC.
Deskriptorji		CREUTZFELDT-JAKOB SYNDROME PRPC PROTEINS PEPTIDES RECOMBINANT PROTEINS PROTEIN STRUCTURE, TERTIARY PROTEIN CONFORMATION PRECIPITIN TESTS MICE, INBRED BALB C EPITOPES ENZYME-LINKED IMMUNOSORBENT ASSAY ENDOPEPTIDASE K ELECTROPHORESIS, POLYACRYLAMIDE GEL