U. Roy
Nipah is a virus borne zoonotic disease that mostly occurs in Southeast Asian countries. Nipah virus (NiV) infection is potentially lethal as it can cause fatal encephalitis, and as of now, there are no vaccines or therapeutic treatments for this disease. The highly pathogenic NiV belongs to the Paramyxovirus family and the natural host of NiV is fruit bats of the Pteropodidae family. Though NiV has not been detected in the US, rather recently the Camp Hill virus (CHV) in shrew species was identified in Camp Hill, Alabama. This virus is characteristically similar to Nipah, and belongs to the henipavirus genus that include the Nipah and Hendra viruses. NiV has two surface glycoproteins namely the attachment glycoprotein (NiVG) and the fusion glycoprotein (NiVF). Being associated with host cell attachment and fusion of viral membrane, these glycoproteins tend to facilitate the viral entry to the host cell. The present paper describes the structures of the aforesaid viral glycoproteins based on the available database of protein structures and examines if they have an evolutionary link to other viral glycoproteins. Certain similar glycoproteins found in different countries are also explored. The structure-function relationship for these two NiV glycoproteins are determined using time-based molecular dynamics (MD) simulation. The interfacial ligand-receptor interactions between NiV proteins with human receptor and monoclonal antibody, Fab 66, are examined. A primary motivation for these structural studies is that the results might potentially contribute to future therapeutic developments and drug designs to effectively combat NiV.