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( Jeongmin Lee ),( Byoung Woo Lee ),( Hae-eun Kang ),( Kevine K. Choe ),( Moosik Kwon ),( Chongsuk Ryou ) 한국미생물 · 생명공학회 2017 Journal of microbiology and biotechnology Vol.27 No.5
The conformational change of cellular prion protein (PrP<sup>C</sup>) to its misfolded counterpart, termed PrP<sup>Sc</sup>, is mediated by a hypothesized cellular cofactor. This cofactor is believed to interact directly with certain amino acid residues of PrP<sup>C</sup>. When these are mutated into cationic amino acid residues, PrPSc formation and prion replication halt in a dominant negative (DN) manner, presumably due to strong binding of the cofactor to mutated PrP<sup>C</sup>, designated as DN PrP mutants. Previous studies demonstrated that plasminogen and its kringle domains bind to PrP and accelerate PrP<sup>Sc</sup> generation. In this study, in vitro binding analysis of kringle domains of plasminogen to Q167R DN mutant PrP (PrPQ167R) was performed in parallel with the wild type (WT) and Q218K DN mutant PrP (PrPQ218K). The binding affinity of PrPQ167R was higher than that of WT PrP, but lower than that of PrPQ218K. Scatchard analysis further indicated that, like PrPQ218K and WT PrP, PrPQ167R interaction with plasminogen occurred at multiple sites, suggesting cooperativity in this interaction. Competitive binding analysis using L-lysine or L-arginine confirmed the increase of the specificity and binding affinity of the interaction as PrP acquired DN mutations. Circular dichroism spectroscopy demonstrated that the recombinant PrPs used in this study retained the α-helix-rich structure. The α-helix unfolding study revealed similar conformational stability for WT and DN-mutated PrPs. This study provides an additional piece of biochemical evidence concerning the interaction of plasminogen with DN mutant PrPs.
( Muhammad Waqas ),( Huyen Trang Trinh ),( Sungeun Lee ),( Dae-hwan Kim ),( Sang Yeol Lee ),( Kevin K. Choe ),( Chongsuk Ryou ) 한국미생물 · 생명공학회 2018 Journal of microbiology and biotechnology Vol.28 No.12
Based on previous studies reporting the anti-prion activity of poly-L-lysine and poly-Larginine, we investigated cationic poly-L-ornithine (PLO), poly-L-histidine (PLH), anionic poly-L-glutamic acid (PLE) and uncharged poly-L-threonine (PLT) in cultured cells chronically infected by prions to determine their anti-prion efficacy. While PLE and PLT did not alter the level of PrP<sup>Sc</sup>, PLO and PLH exhibited potent PrP<sup>Sc</sup> inhibition in ScN2a cells. These results suggest that the anti-prion activity of poly-basic amino acids is correlated with the cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that the anti-prion activity of poly-basic amino acids is associated with their acidic cellular compartments.