BackgroundThe common event in transmissible spongiform encephalopathies (TSEs) or prion diseases is the conversion of host-encoded protease sensitive cellular prion protein (PrPC) into strain dependent isoforms of scrapie associated protease resistant isoform (PrPSc) of prion protein (PrP). These processes are determined by similarities as well as strain dependent variations in the PrP structure. Selective self-interaction between PrP molecules is the most probable basis for initiation of these processes, potentially influenced by chaperone molecules, however the mechanisms behind these processes are far from understood. We previously determined that polymorphisms do not affect initial PrPC to PrPSc binding but rather modulate a subsequent step in the conversion process. Determining possible sites of self-interaction could elucidate which amino acid(s) or amino acid sequences contribute to binding and further conversion into other isoforms. To this end, ovine – and bovine PrP peptide-arrays consisting of 15-mer overlapping peptides were probed with recombinant sheep PrPC fused to maltose binding protein (MBP-PrP).
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机译：背景传染性海绵状脑病（TSEs）或病毒病的常见事件是宿主编码的蛋白酶敏感细胞病毒蛋白（PrP C ）转化为瘙痒病相关蛋白酶抗性同工型（PrP ）。这些过程由PrP结构中的相似性以及应变相关的变化决定。 PrP分子之间的选择性自相互作用是引发这些过程的最可能基础，可能受到分子伴侣分子的影响，但是这些过程背后的机制尚不清楚。我们先前确定多态性不会影响初始PrP C 与PrP Sc 的绑定，而是会影响转换过程中的后续步骤。确定可能的自我相互作用位点可以阐明哪些氨基酸或氨基酸序列有助于结合并进一步转化为其他同工型。为此，用融合有麦芽糖结合蛋白（MBP-PrP）的重组绵羊PrP 探测了由15-mer重叠肽组成的绵羊和牛PrP肽阵列。
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