Abstract
BackgroundAssociation of Epstein-Barr virus (EBV) encoded latent gene products with host ribosomal proteins (RPs) has not been fully explored, despite their involvement in the aetiology of several human cancers. To gain an insight into their plausible interactions, we employed a computational approach that encompasses structural alignment, gene ontology analysis, pathway analysis, and molecular docking.ResultsIn this study, the alignment analysis based on structural similarity allows the prediction of 48 potential interactions between 27 human RPs and the EBV proteins EBNA1, LMP1, LMP2A, and LMP2B. Gene ontology analysis of the putative protein-protein interactions (PPIs) reveals their probable involvement in RNA binding, ribosome biogenesis, metabolic and biosynthetic processes, and gene regulation. Pathway analysis shows their possible participation in viral infection strategies (viral translation), as well as oncogenesis (Wnt and EGFR signalling pathways). Finally, our molecular docking assay predicts the functional interactions of EBNA1 with four RPs individually: EBNA1-eS10, EBNA1-eS25, EBNA1-uL10 and EBNA1-uL11.ConclusionThese interactions have never been revealed previously via either experimental or in silico approach. We envisage that the calculated interactions between the ribosomal and EBV proteins herein would provide a hypothetical model for future experimental studies on the functional relationship between ribosomal proteins and EBV infection.
Highlights
Association of Epstein-Barr virus (EBV) encoded latent gene products with host ribosomal proteins (RPs) has not been fully explored, despite their involvement in the aetiology of several human cancers
In silico identification of RPs that interact with EBV proteins The best 3-D structural models of EBV proteins generated using I-TASSER (Fig. 1) were selected based on the qualities of geometrical and stereochemical parameters (Table 1)
Further analysis using data from Human Protein Reference Database (HPRD) and IntAct, demonstrated these Human proteins structurally similar to EBV proteins (hEBV) to be associated with nearly five thousand human proteins
Summary
Association of Epstein-Barr virus (EBV) encoded latent gene products with host ribosomal proteins (RPs) has not been fully explored, despite their involvement in the aetiology of several human cancers. Ribosomal protein s27a (eS31), on the other hand, interacts with and regulates the stability of EBV-encoded latent membrane protein 1 (LMP1) by inhibiting proteasome-mediated ubiquitination [5]. These findings represent a scant insight of the complete repertoire of functional interactions between the proteins of EBV and ribosome, of which is yet to be fully explored. Protein-protein binding assays and associated functional studies of the 80 known human RPs and 9 EBV proteins will undoubtedly be a resource-intensive and time-consuming endeavour if experimental approach is the only means of study
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