Title

Computational identification of the post-translational modification sites and the functional family prediction reveals possible moonlighting role of rotaviral proteins

Authors

Shiladitya Chattopadhyay¹, Parikshit Bagchi¹, Dipanjan Dutta¹, Anupam Mukherjee¹, Nobumichi Kobayashi², Mamta Chawlasarkar^1*

Affiliation

¹Division of Virology, National Institute of Cholera and Enteric Diseases, P-33, C.I.T. Road Scheme- XM, Beliaghata, Kolkata-700010,India; ²Department of Hygeine, Sapporo Medical University, S-1 W-17, Chuo-ku, Sapporo 060-8556, Japan.

Email

chawlam70@gmail.com

Article Type

Hypothesis

Date

Received February 02, 2010 ; accepted March 02, 2010 ; published April 30, 2010

Abstract

Rotavirus (RV) diarrhoea causes huge number deaths in children less than 5 years of age. In spite of available vaccines, it has been difficult to combat RV due to large number of antigenically distinct genotypes, high mutation rates, generation of reassortant viruses due to segmented genome. RV is an eukaryotic virus which utilizes host cell machinery for its propagation. Since RV only encodes 12 proteins, post-translational modification (PTM) is important mechanism for modification, which consequently alters their function. A single protein exhibiting different functions in different locations or in different subcellular sites, are known to be ‘moonlighting’. So there is a possibility that viral proteins moonlight in separate location and in different time to exhibit diverse cellular effects. Based on the primary sequence, the putative behaviour of proteins in cellular environment can be predicted, which helps to classify them into different functional families with high reliability score. In this study, sites for phosphorylation, glycosylation and SUMOylation of the six RV structural proteins (VP1, VP2, VP3, VP4, VP6 & VP7) & five non-structural proteins (NSP1, NSP2,NSP3,NSP4 & NSP5) and the functional families were predicted. As NSP6 is a very small protein and not required for virus growth & replication, it was not included in the study. Classification of RV proteins revealed multiple putative functions of each structural protein and varied number of PTM sites, indicating that RV proteins may also moonlight depending on requirements during viral life cycle. Targeting the crucial PTM sites on RV structural proteins may have implications in developing future anti-rotaviral strategies.

Keywords

Citation

Chattopadhyay et al., Bioinformation 4(10): 000-000 (2010)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.