Oligomeric forms of peptide fragment PrP(214–226) in solution are preferentially recognized by PrP^Sc-specific antibody

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• 作者：Nataš ; a Poklar Ulrih ; Mihaela Skrt ; Peter Veranič ; Vesna Galvani ; Tanja Vranac and Vladka Č ; urin Š ; erbec
• 关键词：Monoclonal PrP^Sc specific antibody ; Prion protein ; Specific epitope ; Amyloid-like fibrils
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2006
• 出版时间：16 June 2006
• 年：2006
• 卷：344
• 期：4
• 页码：1320-1326
• 全文大小：271 K

文摘

A specific monoclonal antibody (mAb) V5B2 that discriminates between brain tissue of Creutzfeldt–Jakob disease patients and that from normal controls without proteinase K digestion has been prepared using a 13-residue synthetic peptide P1 from the primary structure of human PrP. In the light of the specific interaction between mAb V5B2 and the pathological isoform of PrP (PrP^Sc), we investigated the solution behavior of antigen P1 and its interactions with mAb V5B2. Our results show that V5B2 recognizes epitope P1 in dimeric/oligomeric forms in solution and in the fibril-like aggregates, as well as in PrP^Sc aggregates, and demonstrate that the specific epitope is present in all of these forms, but not in PrP^C.