In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins
Background 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. To gain an insight into their plausible interactions, we employed a computational appr...
Saved in:
Main Authors: | , |
---|---|
Format: | Article |
Language: | English |
Published: |
Springer Nature
2019
|
Subjects: | |
Online Access: | http://ir.unimas.my/id/eprint/26506/1/talwar.pdf http://ir.unimas.my/id/eprint/26506/ https://bmcmolcellbiol.biomedcentral.com/articles/10.1186/s12860-019-0219-y |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Universiti Malaysia Sarawak |
Language: | English |
id |
my.unimas.ir.26506 |
---|---|
record_format |
eprints |
spelling |
my.unimas.ir.265062021-04-27T13:36:27Z http://ir.unimas.my/id/eprint/26506/ In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins Sim, Edmund Ui Hang Talwar, Prashant Shruti QH301 Biology Background 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. 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. Results In 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. Conclusion These 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. Springer Nature 2019-08-15 Article PeerReviewed text en http://ir.unimas.my/id/eprint/26506/1/talwar.pdf Sim, Edmund Ui Hang and Talwar, Prashant Shruti (2019) In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins. BMC Molecular and Cell Biology, 20 (34). pp. 1-12. ISSN 2661-8850 https://bmcmolcellbiol.biomedcentral.com/articles/10.1186/s12860-019-0219-y DOI :10.1186/s12860-019-0219-y |
institution |
Universiti Malaysia Sarawak |
building |
Centre for Academic Information Services (CAIS) |
collection |
Institutional Repository |
continent |
Asia |
country |
Malaysia |
content_provider |
Universiti Malaysia Sarawak |
content_source |
UNIMAS Institutional Repository |
url_provider |
http://ir.unimas.my/ |
language |
English |
topic |
QH301 Biology |
spellingShingle |
QH301 Biology Sim, Edmund Ui Hang Talwar, Prashant Shruti In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
description |
Background
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. 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.
Results
In 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.
Conclusion
These 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. |
format |
Article |
author |
Sim, Edmund Ui Hang Talwar, Prashant Shruti |
author_facet |
Sim, Edmund Ui Hang Talwar, Prashant Shruti |
author_sort |
Sim, Edmund Ui Hang |
title |
In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
title_short |
In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
title_full |
In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
title_fullStr |
In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
title_full_unstemmed |
In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins |
title_sort |
in silico evidence of de novo interactions between ribosomal and epstein - barr virus proteins |
publisher |
Springer Nature |
publishDate |
2019 |
url |
http://ir.unimas.my/id/eprint/26506/1/talwar.pdf http://ir.unimas.my/id/eprint/26506/ https://bmcmolcellbiol.biomedcentral.com/articles/10.1186/s12860-019-0219-y |
_version_ |
1698700795819589632 |