title: Cytotoxic Activities of Eosinophil Cationic Protein and Eosinophil-derived Neurotoxin: In Silico Analysis.
abstract: 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.
  
  
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Laboratory of Molecular Biology, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil.
authors.forename: Paula Cristina Rabelo
authors.initials: PC
authors.lastname: De Oliveira
authors.affiliation: Laboratory of Molecular Biology, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil.
authors.forename: Débora
authors.initials: D
authors.lastname: De Oliveira Lopes
authors.affiliation: Laboratory of Molecular Modeling, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil.
authors.forename: Ivan Evangelista
authors.initials: IE
authors.lastname: Do Vale Coelho
authors.affiliation: Laboratory of Molecular Biology, Federal University of São João Del Rei-Midwest Campus Dona Lindu, Divinópolis, Brazil michelepereira@ufsj.edu.br.
authors.forename: Michele Conceição
authors.initials: MC
authors.lastname: Pereira
mesh_terms: D001120:Arginine / Q000737:chemistry; D019295:Computational Biology; D030562:Databases, Protein; D047150:Eosinophil Cationic Protein / Q000378:metabolism*; D047208:Eosinophil-Derived Neurotoxin / Q000378:metabolism*; D005786:Gene Expression Regulation; D005973:Glutamine / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012984:Software
chemical_list: D005973:Glutamine; D001120:Arginine; D047208:Eosinophil-Derived Neurotoxin; D047150:Eosinophil Cationic Protein; D012259:Ribonuclease, Pancreatic
keywords: Eosinophil cationic protein; bioinformatics; eosinophil-derived neurotoxin; homology; post-translational modifications