Abstract
Hepatitis E virus (HEV) is the causative agent of Hepatitis E infections across the world. Intrinsically disordered protein regions (IDPRs) or intrinsically disordered proteins (IDPs) are regions or proteins that are characterized by lack of definite structure. These IDPRs or IDPs play significant roles in a wide range of biological processes, such as cell cycle regulation, control of signaling pathways, etc. IDPR/IDP in proteins is associated with the virus's pathogenicity and infectivity. The prevalence of IDPR/IDP in rat HEV proteome remains undetermined. Hence, we examined the unstructured/disordered regions of the open reading frame (ORF) encoded proteins of rat HEV by analyzing the prevalence of intrinsic disorder. The intrinsic disorder propensity analysis showed that the different ORF proteins consisted of varying fraction of intrinsic disorder. The protein ORF3 was identified with maximum propensity for intrinsic disorder while the ORF6 protein had the least fraction of intrinsic disorder. The analysis revealed ORF6 as a structured protein (ORDP); ORF1 and ORF4 as moderately disordered proteins (IDPRs); and ORF3 and ORF5 as highly disordered proteins (IDPs). The protein ORF2 was found to be moderately as well as highly disordered using different predictors, thus, was categorized into both IDPR and IDP. Such disordered regions have important roles in pathogenesis and replication of viruses.
Highlights
The analysis revealed ORF6 as a structured protein (ORDP); ORF1 and ORF4 as moderately disordered proteins (IDPRs); and ORF3 and ORF5 as highly disordered proteins (IDPs)
Hepatitis E is inflammation of the liver which is caused by the Hepatitis E virus (HEV) [1 ]
The proteins or protein regions that fail to get folded into definite three-dimensional (3D) structures but remain biologically active are termed as intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs), respectively [13 - 15]
Summary
Hepatitis E is inflammation of the liver which is caused by the Hepatitis E virus (HEV) [1 ]. Recent studies have determined the role of different reading frame encoded proteins in HEV regulation by analyzing their intrinsically disordered regions [6 9], as these regions are linked with virus’s infection and pathogenesis [10 - 12]. The proteins or protein regions that fail to get folded into definite three-dimensional (3D) structures but remain biologically active are termed as intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs), respectively [13 - 15]. These disordered protein regions exist as extremely active ensembles that are rapidly interconvertible under different physiological conditions [13 - 15]. It is of interest to document the intrinsically disordered regions in the rodent hepevirus proteome
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