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Description
Nipah virus is a highly pathogenic bat-borne virus that occasionally spills over into humans. The NiV receptor binding protein (RBP) binds host receptors during cell entry and is a target of neutralizing antibodies, which can protect against disease. Here, we experimentally measure the effects of all amino acid-mutations in the RBP on three viral phenotypes: cell entry, receptor binding, and antibody neutralization. We identify constrained regions which are essential for cell entry and mutations that modulate binding of RBP to its two cellular receptors, ephrinB2 and B3. Finally, we map all potential escape mutations to six clinically relevant mAbs but show most of these mutations are not present in known natural Nipah virus strains, suggesting Nipah may be more antigenically conserved than some other RNA viruses. Our findings offer crucial insights into the functional and antigenic evolution of Nipah.
