Cell-cell fusion (syncytia) in lung, brain, kidney, and heart tissues is caused by Nipah (NiV) and Hendra (HeV) viruses. This results in encephalitis, pneumonia, and frequent death. Henipavirus infections are characterized by membrane fusion, which is required for viral entry and virusinduced cell-cell fusion . Understanding the pathobiology of henipaviruses relies on elucidating the mechanism(s) of membrane fusion, which may lead to discovering new approaches to creating antiviral therapeutics. Viral attachment (G) and fusion (F) glycoproteins must work together to facilitate membrane fusion in henipaviruses. Current theories of henipavirus fusion propose that F is released from its metastable pre-fusion conformation to promote membrane fusion after NiV or HeV G attachment to its cell surface receptors . The selected protein for this study is a fusion protein of Nipah henipavirus associated with viral infections. The physicochemical characteristics and anticipated protein structures of the selected protein demonstrated structure-function relationships of the proteins associated with viral infections. Therefore, this protein can be targeted for predicting antiviral drugs and vaccines against the selected protein to combat viral infections.