Structures and Activities of Prions and Prion Proteins

朊病毒和朊病毒蛋白的结构和活性

• 批准号: 8156862
• 负责人: BYRON CAUGHEY
• 金额: $ 147.52万
• 依托单位: NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/8156862
• 关键词: Prions; Structure

Accomplishments for FY2010: 1) We have extended our experimental support for the conclusion that mammalian prions that cause a transmissible spongiform encephalopathy (TSE or prion disease) can be generated solely from bacterially expressed recombinant prion protein. This discovery provides the most compelling evidence so far for the potential protein-only prion hypothesis for the nature of the TSE infectious agent. However, the data leave open the likelihood that other molecules strongly enhance the infectious titers of pathological forms of prion protein. 2) We have studied the strain-dependent structures of prion seeded recombinant PrP fibrils. 3) We have extended our characterization of TSE strain-dependent differences in the interactions between prion protein and complement factors. 4) We have probed the effects of glycosylation and GPI-anchoring on the conformations of different strains of scrapie-prion protein by infrared spectroscopy. 5) We have studied cellular effects of nucleic acid binding to normal prion protein.

2010财年的成就：1）我们扩展了我们的实验支持，以结论，即引起可传播的海绵状脑病（TSE或PRION病）的哺乳动物prions可以单独由细菌表达的重组prion蛋白产生。这一发现为迄今为止的最引人注目的证据提供了针对TSE感染剂性质的潜在唯一蛋白质prion假说。但是，数据离开开放的可能性是其他分子强烈增强病毒蛋白质形式的传染性滴度。 2）我们研究了pr菌的重组PRP原纤维的应变依赖性结构。 3）我们扩展了对prion蛋白与补体因子之间相互作用的TSE应变依赖性差异的表征。 4）我们已经探测了糖基化和gpi锚定对红外光谱蛋白不同菌株的构象的影响。 5）我们研究了核酸与正常pr蛋白结合的细胞作用。