IN-SILICO MOLECULAR ANALYSIS AND BLOCKING OF THE VIRAL G PROTEIN OF NIPAH VIRUS INTERACTING WITH EPHRIN B2 AND B3 RECEPTOR BY USING PEPTIDE MASS FINGERPRINTING

Ayesha Sajjad¹ihteshamul Haq^2*Rabia Syed¹Faheem Anwar³Muhammad Hamza¹Faisal Nouroz⁴Tehmina Kiani¹

• ¹Department of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, KP, Pakistan, Abbotabad, Pakistan
• ²College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, Beijing Municipality, China
• ³Academy of Medical Engineering and Translational Medicine, Tianjin University, Tianjin, China
• ⁴Department of Bioinformatics, Faculty of Sciences, Hazara University, Dhodial, Khyber Pakhtunkhwa, Pakistan

The Nipah virus (NiV), a zoonotic paramyxovirus closely related to the Hendra virus, poses a significant global health threat due to its high mortality rate, zoonotic nature, and recurring outbreaks primarily in Malaysia, Bangladesh, and India. Infection with NiV leads to severe encephalitis and carries a case fatality rate ranging from 40% to 75%. The lack of a vaccine and limited understanding of NiV pathogenesis underscore the urgent need for effective therapeutics. This study focuses on identifying viral peptides of the Nipah virus using the peptide mass fingerprinting technique. Through this approach, antiviral peptides acting as potent inhibitors were identifiedThis approach identified antiviral peptides acting as potent inhibitors, targeting the viral G-protein's interaction with cellular ephrin-B2 and B3 receptors. These receptors are crucial for viral entry into host cells and subsequent pathogenesis. The identification ofIdentifying NiV viral peptides not only enhances our understanding of the virus's structural and functional properties but also opens avenues for developing novel therapeutic strategies. By blocking the interaction between the viral G-protein and host receptors, these antiviral peptides offer promising prospects for drug development against NiV. Twenty-one peptides were identified using peptide mass fingerprinting. These peptides were then subjected to docking analysis with two antiviral peptides of the ephrin B2 receptor and a monoclonal antibody, demonstrating robust stability and binding affinity. These predicted peptides contribute to the broader field of virology by elucidating key aspects of NiV biology Formatted: Superscript and paving the way for the development of targeted antiviral therapies. Future studies may further explore the therapeutic potential of these peptides and their application in combating other viral infections.