Amyloid properties of the mouse egg zona pellucida.
Amyloid properties of the mouse egg zona pellucida.
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DOI：
10.1371/journal.pone.0129907
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发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Cornwall GA
中科院分区：
文献类型：
--
作者：
Egge N;Muthusubramanian A;Cornwall GA
卵母细胞周围的透明质膜（ZP）是一种细胞外纤维基质，在受精过程中起着关键作用，包括种特异性配子识别和保护多精受精。小鼠ZP由三种蛋白质ZP 1、ZP 2和ZP 3组成，它们都具有ZP聚合结构域，该结构域指导蛋白质原纤维形成和组装成三维ZP基质。在非哺乳类脊椎动物和无脊椎动物中卵母细胞周围的卵被也是纤维状基质，并且由含有ZP结构域的蛋白组成，这表明ZP/卵被的基本结构和功能是高度保守的。然而，ZP结构域之间的序列相似性在物种间较低，因此ZP/蛋壳结构及其功能的保守机制尚不清楚。使用经典的方法来识别淀粉样蛋白，包括构象依赖性抗体和染料，X射线衍射，负染色电子显微镜，我们的研究表明，小鼠ZP是一个功能性淀粉样蛋白。淀粉样蛋白是交叉β折叠的纤维状结构，其虽然通常与哺乳动物中的神经退行性疾病和朊病毒疾病相关，但也可以在正常细胞中发挥功能作用而不导致病理学。使用算法AmylPred 2对来自小鼠ZP 3和来自另外五个分类群的ZP 3同系物的ZP结构域进行分析以鉴定淀粉样蛋白生成位点，揭示了在所有分类群中预测形成淀粉样蛋白的区域的显著保守性。这包括一个保守的淀粉样蛋白生成区域，该区域定位于先前在小鼠ZP 3中显示的一段疏水氨基酸，这对于原纤维组装是必需的。类似地，酵母蛋白α-凝集素/Sag 1 p中的一个结构域具有ZP结构域样特征，并且是交配所必需的，也具有预测为淀粉样蛋白生成的位点，包括似乎类似于小鼠ZP 3中关键位点的疏水性延伸。总之，这些研究表明，淀粉样蛋白的形成可能是一个保守的机制，ZP的结构和功能在数十亿年的进化。
The zona pellucida (ZP) surrounding the oocyte is an extracellular fibrillar matrix that plays critical roles during fertilization including species-specific gamete recognition and protection from polyspermy. The mouse ZP is composed of three proteins, ZP1, ZP2, and ZP3, all of which have a ZP polymerization domain that directs protein fibril formation and assembly into the three-dimensional ZP matrix. Egg coats surrounding oocytes in nonmammalian vertebrates and in invertebrates are also fibrillar matrices and are composed of ZP domain-containing proteins suggesting the basic structure and function of the ZP/egg coat is highly conserved. However, sequence similarity between ZP domains is low across species and thus the mechanism for the conservation of ZP/egg coat structure and its function is not known. Using approaches classically used to identify amyloid including conformation-dependent antibodies and dyes, X-ray diffraction, and negative stain electron microscopy, our studies suggest the mouse ZP is a functional amyloid. Amyloids are cross-β sheet fibrillar structures that, while typically associated with neurodegenerative and prion diseases in mammals, can also carry out functional roles in normal cells without resulting pathology. An analysis of the ZP domain from mouse ZP3 and ZP3 homologs from five additional taxa using the algorithm AmylPred 2 to identify amyloidogenic sites, revealed in all taxa a remarkable conservation of regions that were predicted to form amyloid. This included a conserved amyloidogenic region that localized to a stretch of hydrophobic amino acids previously shown in mouse ZP3 to be essential for fibril assembly. Similarly, a domain in the yeast protein α-agglutinin/Sag 1p, that possesses ZP domain-like features and which is essential for mating, also had sites that were predicted to be amyloidogenic including a hydrophobic stretch that appeared analogous to the critical site in mouse ZP3. Together, these studies suggest that amyloidogenesis may be a conserved mechanism for ZP structure and function across billions of years of evolution.
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影响因子：
15.1
作者：
Kayed R;Canto I;Breydo L;Rasool S;Lukacsovich T;Wu J;Albay R 3rd;Pensalfini A;Yeung S;Head E;Marsh JL;Glabe C
通讯作者：
Glabe C
影响因子：
5.8
作者：
Callebaut, Isabelle;Mornon, Jean-Paul;Monget, Philippe
通讯作者：
Monget, Philippe
DOI：
10.1073/pnas.0603125103
发表时间：
2006-11-14
影响因子：
11.1
作者：
Aagaard, Jan E.;Yi, Xianhua;Swanson, Willie J.
通讯作者：
Swanson, Willie J.
影响因子：
4.8
作者：
Legan, PK;Rau, A;Richardson, GP
通讯作者：
Richardson, GP
DOI：
10.1073/pnas.0401600101
发表时间：
2004-04-20
影响因子：
11.1
作者：
Jovine, L;Qi, HY;Wassarman, PM
通讯作者：
Wassarman, PM