De Oliveira Paula Cristina Rabelo, De Oliveira Lopes Débora, Do Vale Coelho Ivan Evangelista, Pereira Michele Conceição
Laboratory of Molecular Biology, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil.
Laboratory of Molecular Modeling, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil.
Cancer Genomics Proteomics. 2015 Nov-Dec;12(6):397-402.
Eosinophil cationic protein (ECP) and eosinophil derived-neurotoxin (EDN) are homologous ribonuclease (RNAse) A family proteins. The objective of the present study was to in silico characterize ECP and EDN with respect to their cytotoxic activities.
Structural, physicochemical, and conserved domain characterizations were carried-out using open-source software, such as InterProScan, NetOGlyc, NetPhos and Discovery Studio 3.1.
The proteins did not have atypical conserved domains. EDN had a greater number of glutamine amino acid residues, whereas ECP had a predominance of arginine. ECP had four possible N-glycosylation, three O-glycosylation and four phosphorylation sites. EDN had five putative N-glycosylation, three phosphorylation and no O-glycosylation sites.
The greater cationicity of ECP may be related to its higher cytotoxicity and to the fact that the varying post-translational modification profiles can generate functional differences from structural alteration. In vivo and in vitro studies need to be performed in order to confirm these predictions.
嗜酸性粒细胞阳离子蛋白（ECP）和嗜酸性粒细胞衍生神经毒素（EDN）是同源的核糖核酸酶（RNAse）A家族蛋白。本研究的目的是在计算机上对ECP和EDN的细胞毒性活性进行表征。
使用诸如InterProScan、NetOGlyc、NetPhos和Discovery Studio 3.1等开源软件进行结构、物理化学和保守结构域表征。
这些蛋白质没有非典型的保守结构域。EDN具有更多数量的谷氨酰胺氨基酸残基，而ECP以精氨酸为主。ECP有四个可能的N-糖基化、三个O-糖基化和四个磷酸化位点。EDN有五个推定的N-糖基化、三个磷酸化且没有O-糖基化位点。
ECP较高的阳离子性可能与其较高的细胞毒性有关，并且不同的翻译后修饰谱可通过结构改变产生功能差异。需要进行体内和体外研究以证实这些预测。
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