Polanco Carlos, Samaniego Mendoza José Lino, Buhse Thomas, Uversky Vladimir N, Bañuelos Chao Ingrid Paola, Bañuelos Cedano Marcela Angola, Tavera Fernando Michel, Tavera Daniel Michel, Falconi Manuel, Ponce de León Abelardo Vela
Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, Av. Universidad 3000, México City, 04510, Mexico.
Centro de Investigaciones Químicas, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Chamilpa, Cuernavaca, 62209, Mexico.
Cell Biochem Biophys. 2018 Sep;76(3):411-431. doi: 10.1007/s12013-018-0839-4. Epub 2018 Mar 6.
The number of fatalities and economic losses caused by the Ebola virus infection across the planet culminated in the havoc that occurred between August and November 2014. However, little is known about the molecular protein profile of this devastating virus. This work represents a thorough bioinformatics analysis of the regularities of charge distribution (polar profiles) in two groups of proteins and their functional domains associated with Ebola virus disease: Ebola virus proteins and Human proteins interacting with Ebola virus. Our analysis reveals that a fragment exists in each of these proteins-one named the "functional domain"-with the polar profile similar to the polar profile of the protein that contains it. Each protein is formed by a group of short sub-sequences, where each fragment has a different and distinctive polar profile and where the polar profile between adjacent short sub-sequences changes orderly and gradually to coincide with the polar profile of the whole protein. When using the charge distribution as a metric, it was observed that it effectively discriminates the proteins from their functional domains. As a counterexample, the same test was applied to a set of synthetic proteins built for that purpose, revealing that any of the regularities reported here for the Ebola virus proteins and human proteins interacting with Ebola virus were not present in the synthetic proteins. Our results indicate that the polar profile of each protein studied and its corresponding functional domain are similar. Thus, when building each protein from its functional domai-adding one amino acid at a time and plotting each time its polar profile-it was observed that the resulting graphs can be divided into groups with similar polar profiles.
2014年8月至11月期间，埃博拉病毒感染在全球范围内造成的死亡人数和经济损失达到顶峰，这场浩劫令人触目惊心。然而，对于这种极具破坏力的病毒的分子蛋白特征，我们却知之甚少。这项研究对两组与埃博拉病毒病相关的蛋白质及其功能结构域的电荷分布规律（极性图谱）进行了全面的生物信息学分析，这两组蛋白质分别是：埃博拉病毒蛋白以及与埃博拉病毒相互作用的人类蛋白。我们的分析表明，这些蛋白质中的每一个都存在一个片段——我们称之为“功能结构域”，其极性图谱与包含它的蛋白质的极性图谱相似。每个蛋白质由一组短子序列组成，其中每个片段都有不同且独特的极性图谱，相邻短子序列之间的极性图谱会有序且逐渐地变化，以与整个蛋白质的极性图谱相契合。当以电荷分布作为衡量标准时，我们发现它能够有效地将蛋白质与其功能结构域区分开来。作为反例，我们对一组为此目的构建的合成蛋白质进行了同样的测试，结果显示，在此报道的埃博拉病毒蛋白和与埃博拉病毒相互作用的人类蛋白的任何规律在合成蛋白质中均不存在。我们的结果表明，所研究的每种蛋白质及其相应功能结构域的极性图谱是相似的。因此，当从其功能结构域构建每种蛋白质时——每次添加一个氨基酸并每次绘制其极性图谱——我们观察到所得的图谱可以分为具有相似极性图谱的组。
