Background: 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.
Materials and methods: Structural, physicochemical, and conserved domain characterizations were carried-out using open-source software, such as InterProScan, NetOGlyc, NetPhos and Discovery Studio 3.1.
Results: 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.
Conclusion: 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.
Keywords: Eosinophil cationic protein; bioinformatics; eosinophil-derived neurotoxin; homology; post-translational modifications.
Copyright© 2015, International Institute of Anticancer Research (Dr. John G. Delinasios), All rights reserved.