Abstract Nipah virus is a highly pathogenic virus in the family Paramyxoviridae that utilizes two distinct surface glycoproteins to infect cells . The receptor-binding protein (RBP) binds host receptors whereas the fusion protein (F) merges viral and host membranes . Here, we use nonreplicative pseudoviruses to safely measure the effects of all F single amino acid residue mutations on its cell entry function and neutralization by monoclonal antibodies . We compare mutational tolerance in F with previous experimental measurements for RBP and show that F is much more functionally constrained than the RBP . We also identify mutationally intolerant sites on the F trimer surface and core that are critical for proper function, and describe mutations that are candidates for stabilizing F in the prefusion conformation for vaccine design . We quantify how F mutations affect neutralization by six monoclonal antibodies, and show that the magnitude of mutational effects on neutralization var...
Media Monitoring for Signals about Emerging Threats