Pages: 10-17

Abstract

The VP35 protein in Ebola virus is one of the main pathogenic components interacting to host cells and interferes with natural cellular immune responses. This is done by antagonistic potential of the viral VP35 protein which inhibits interferon regulatory factor 3 (IRF-3) protein in the infected cells and then induction of antiviral genes expression is disrupted. In the present in silico study, we have designed a novel recombinant IFNα/β receptor protein which can be secreted out by host cells and circulate in blood stream. Methods: the amino acid sequence of IFNα/β was taken from NCBI, to design the recombinant IFNα/β protein, functional, biophysical properties of VP35, and conserved domains were identified by Pfam and ProDom website. Few cystein amino acids were added to the adjacent region of identified domains to form disulfide bonds with possible cysteins present in VP35 polypeptide chains. The hydrophobicity index and net charge of the protein were studies by GPMAW and PepDraw website. For available signal peptide sequence are predicted by SignalP website and also conserved regions are identified by ClustalO. Next, to investigate the function of recombinant protein, the gene network involved in protein features functional pathways was identified by STRING and UCSF software. Result: When the body encounters the virus, the recombinant protein can bind to VP35 and inhibit its antagonistic effect on IRF-3 proteins. We found instability index (57.47), Aliphatic index (85.50), Hydrophobicity index o (GPMAW as -0.276 Kcal/mol). Conclusion: Evaluations made by bioinformatics software’s revealed that the novel recombinant protein show promise for ameliorating the virulence of Ebola. But the obtained results should be investigated in vitro and in vivo for further evaluation and possible approval as a therapeutic strategy. These investigations are carried out to suggest a novel and efficient therapeutic approach for treatment of Ebola virus-mediated disease condition