Abstract
Introduction:The Japanese Encephalitis Virus (JEV) causes the acute inflammatory disease of the central nervous system known as Japanese encephalitis. JEV is a RNA virus (+strand) that is tiny, enclosed, and from the family Flavivirus. The envelope protein (E), which facilitates JEV entrance into the host cell, has been chosen as a possible molecular aim for therapeutic progress in this work. Materials and Methods:The 3D structure of E protein was retrieved from RCSB PDB (id: 3P54). The sdf files of four lead molecules namely etoposide, netropsin, nogalamycin, and novobiocin were downloaded from the PubChem and used for molecular docking against JEV E protein. We then assessed the fluorescence emission intensity of JEV alone and JEV bound to novobiocin at 280-500 nM to confirm the inhibition of JEV by Novobiocin. The secondary structure of JEV was ascertained by measuring its CD spectra. The CD spectra of JEV were examined as a function of temperature to evaluate the protein constancy. Results: Our docking and fluorescence emission spectra results showed that JEV E pro has good binding preference for novobiocin among these four test compounds. Moreover, fluorescence emission spectra of JEV E protein with novobiocin also revealed the 5 mu M concentration is an effective novobiocin concentration to inhibit the activity of target protein. One top ranked lead molecule namely novobiocin with strong binding affinity (-8.574 Kcal/mol) to JEV E protein was known based on binding energy. Results of the CD Spectra made it quite evident that there is no random coil. Peaks in the negative range (troughs) at 210-230 nm in the CD spectra indicate that JEV has a secondary structure rich in helices. The data unambiguously show that there is no appreciable variation in the JEV curves. Conclusion: Conclusion of the current work offer a thorough understanding of how the JEV E protein is inhibited and provide information that will help novobiocin be developed as a therapeutic drug against JEV E protein in certain viral diseases.