Suppr超能文献

克雅氏病和羊瘙痒病中主要肽段的特征分析。

Characterization of major peptides in Creutzfeldt-Jakob disease and scrapie.

作者信息

Sklaviadis T, Manuelidis L, Manuelidis E E

出版信息

Proc Natl Acad Sci U S A. 1986 Aug;83(16):6146-50. doi: 10.1073/pnas.83.16.6146.

Abstract

In Creutzfeldt-Jakob disease three major peptides cosediment with the infectious agent. These distinct peptides are not present in identical fractions from uninfected brain, and bind to polyclonal antibodies raised against "prion protein" purified by protease treatment. Three similar distinct peptides are also found in scrapie-infected brain fractions purified without the use of proteases. To clarify the relationships between these distinct peptides and prion protein, peptides were analyzed on immunoblots after cleavage with various glycosidases. There are two different 34-kDa peptides. One binds to ricin and cannot be detected by nonequilibrium pH gradient electrophoresis, presumably due to its highly acidic or basic pI. A second basic 34-kDa glycopeptide (Gp34) contains multiple terminal sialic acid residues responsible for charge heterogeneity (pI values, 7.2-7.8) and is reduced to a single spot with a pI value of 7.8 after neuraminidase treatment. After (but not before) neuraminidase treatment, secondary D-galactose-like sugars are detectable on Gp34, and a small number of N-acetylglucosamine residues probably represent the third sugar residue in an N-linked chain. When virtually all sugar residues are removed with endoglycosidase H the molecular weight of Gp34 is reduced by only approximately equal to 2 kDa. The residual peptide strongly binds antibody. A third acidic 24- to 26-kDa species (p26) also binds polyclonal antibodies but, in contrast to Gp34, was unaffected by any glycosidase treatment. Protease-treated peptides showed a very broad array of pI spots, consistent with a heterogeneous protein origin. None of the nonproteolyzed peptides show a clear relationship to prion protein. The number of sugar residues on Gp34 is not consistent with those estimated for prion protein. Although p26 could be the source of the "prion sequence," p26 does not appear to be glycosylated. Regardless, it is likely that all the major peptides described thus far are accumulated or modified normal gene products and are not integral components of the infectious agent.

摘要

在克雅氏病中,三种主要肽段与感染因子共同沉降。这些不同的肽段在未感染大脑的相同组分中不存在,并且能与针对经蛋白酶处理纯化的“朊病毒蛋白”产生的多克隆抗体结合。在未经蛋白酶处理纯化的羊瘙痒病感染脑组分中也发现了三种类似的不同肽段。为了阐明这些不同肽段与朊病毒蛋白之间的关系,在用各种糖苷酶切割后,对肽段进行了免疫印迹分析。有两种不同的34 kDa肽段。一种与蓖麻毒素结合,并且通过非平衡pH梯度电泳无法检测到,推测是由于其高度酸性或碱性的等电点。第二种碱性34 kDa糖肽(Gp34)含有多个负责电荷异质性的末端唾液酸残基(等电点值,7.2 - 7.8),并且在神经氨酸酶处理后还原为单个等电点值为7.8的斑点。在神经氨酸酶处理后(但不是之前),在Gp34上可检测到二级D - 半乳糖样糖,并且少量的N - 乙酰葡糖胺残基可能代表N - 连接链中的第三个糖残基。当用内切糖苷酶H几乎去除所有糖残基时,Gp34的分子量仅降低约2 kDa。残留的肽段强烈结合抗体。第三种酸性24至26 kDa物种(p26)也结合多克隆抗体,但与Gp34不同,它不受任何糖苷酶处理的影响。经蛋白酶处理的肽段显示出非常广泛的等电点斑点阵列,这与异质蛋白质来源一致。没有一种未经蛋白酶处理的肽段与朊病毒蛋白有明确的关系。Gp34上的糖残基数量与朊病毒蛋白估计的数量不一致。尽管p26可能是“朊病毒序列”的来源,但p26似乎未被糖基化。无论如何,到目前为止描述的所有主要肽段可能都是积累或修饰的正常基因产物,而不是感染因子的组成部分。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/594d/386456/351ae4870087/pnas00320-0403-a.jpg

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验