Autor: |
Chen, Gao, Ke, Ren, Long-Zhu, Li, Hui-Ying, Jiang, Cao, Chen, Jin, Zhang, Jun, Han, Xiao-Ping, Dong |
Rok vydání: |
2013 |
Předmět: |
|
Zdroj: |
Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology. 26(5) |
ISSN: |
1003-9279 |
Popis: |
To study the conversion of mutant D178N prion protein in RT-QuIC assay.The D178N mutant prion PRNP was generated by the method of single site mutation. The mutant PRNP gene was inserted into plasmids of pET24. The full and N-truncated recombinant human prion proteins were expressed and purified. The fibril formations of these proteins were real-time monitored by the method of RT-QuIC. The ability to resist proteinase K (PK) of these fibrils was analyzed.We succeed to construct human PrP-D178N plamids. The N-truncated human prion protein with D178N (PrP90-231-D178N) can convert spontaneously in RT-QuIC, while full length of human prion D178N protein (PrP23-231-D178N) fails to convert spontaneously. The spontaneously generated fibril has been domenstrated it is partily PK-resistant.The N-terminal of prion protein (23-90) plays an important role for the D178N mutant protein spontaneously conversion, which provide the clues for study the pathogenesis of genetic CJD. |
Databáze: |
OpenAIRE |
Externí odkaz: |
|