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首页> 外文期刊>Prion >PrPSc-specific antibodies do not induce prion disease or misfolding of PrPc in highly susceptible Tga20 mice
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PrPSc-specific antibodies do not induce prion disease or misfolding of PrPc in highly susceptible Tga20 mice

机译:PrPSc特异性抗体不会在高度易感的Tga20小鼠中诱发病毒疾病或PrPc的错误折叠

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摘要

Transmissible spongiform encephalopathies (tSEs) are fatal neurodegenerative disorders caused by misfolding of a cellular protein PrP C into an infectious conformation PrPSc. Previously our group demonstrated induction of PrPSc-specific antibodies with a Sn6b vaccine that targets regions of the protein that are exposed upon misfolding. there are concerns that these antibodies could function as templates to promote misfolding and cause disease. to evaluate the consequences of prolonged exposure to PrPSc-specific antibodies in a prion sensitized animal, tga20 mice were vaccinated with the Sn6b vaccine. no clinical signs of disease were detected up to 255 d post-vaccination, and postmortem assay of brains and spleens revealed no proteinase-K resistant PrP. these results suggest that vaccinating against tSEs with the Sn6b antigen is safe from the standpoint of prion disease induction.
机译:可传播的海绵状脑病(tSEs)是致命的神经退行性疾病,由细胞蛋白PrP C错折叠成感染性构象PrPSc引起。先前,我们的小组证明了用Sn6b疫苗诱导PrPSc特异性抗体的诱导,该疫苗靶向错误折叠时暴露的蛋白质区域。人们担心这些抗体可能充当模板以促进错误折叠并引起疾病。为了评估在a病毒致敏动物中长时间暴露于PrPSc特异性抗体的后果,对tga20小鼠接种了Sn6b疫苗。疫苗接种后255 d仍未检测到疾病的临床体征,脑和脾的死后检测未发现蛋白酶K抗性PrP。这些结果表明,从病毒疾病诱导的角度出发,用Sn6b抗原对tSE进行疫苗接种是安全的。

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