Elucidating the Interacting Domains of Chandipura Virus Nucleocapsid Protein

• Published in: Advances in virology 2013-01, Vol.2013 (2013), p.1-9
• Main Authors: Kumar, Kapila, Rajasekharan, Sreejith, Gulati, Sahil, Rana, Jyoti, Gabrani, Reema, Jain, Chakresh K., Gupta, Amita, Chaudhary, Vijay K., Gupta, Sanjay
• Format: Article
• Language: English
• Subjects: Chandipura virus; Genomes; Protein folding; Rabies; Studies
• ISSN: 1687-8639; 1687-8647
• DOI: 10.1155/2013/594319

The nucleocapsid (N) protein of Chandipura virus (CHPV) plays a crucial role in viral life cycle, besides being an important structural component of the virion through proper organization of its interactions with other viral proteins. In a recent study, the authors had mapped the associations among CHPV proteins and shown that N protein interacts with four of the viral proteins: N, phosphoprotein (P), matrix protein (M), and glycoprotein (G). The present study aimed to distinguish the regions of CHPV N protein responsible for its interactions with other viral proteins. In this direction, we have generated the structure of CHPV N protein by homology modeling using SWISS-MODEL workspace and Accelrys Discovery Studio client 2.55 and mapped the domains of N protein using PiSQRD. The interactions of N protein fragments with other proteins were determined by ZDOCK rigid-body docking method and validated by yeast two-hybrid and ELISA. The study revealed a unique binding site, comprising of amino acids 1–30 at the N terminus of the nucleocapsid protein (N1) that is instrumental in its interactions with N, P, M, and G proteins. It was also observed that N2 associates with N and G proteins while N3 interacts with N, P, and M proteins.