Antigenic and mutational insights into the Nipah virus G glycoprotein: implications for viral entry, host...

Nipah virus (NiV), a highly lethal RNA virus from the Paramyxoviridae family, causes severe neurological and respiratory diseases in humans. First identified during the 1990s outbreak in Malaysia, NiV remains a significant global health threat due to the absence of approved vaccines or antiviral treatments. Since its discovery, more than 754 cases have been reported, with a mortality rate exceeding 50%. Despite its classification as a biosafety level 4 pathogen, the molecular mechanisms underlying NiV pathogenesis remain poorly understood. Two surface glycoproteins-the attachment (G) and fusion (F) proteins-play crucial roles in facilitating early stages of cell entry and determining host specificity. While naturally occurring mutations in the G glycoprotein are limited, experimental studies involving engineered mutations have provided critical insights into receptor binding, fusion activation, and immune evasion. This review summarizes current knowledge of these antigenic and mutational findings, highlighting their implications for viral entry and host specificity, and providing valuable insights for the development of vaccines and therapeutics.