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+---
+layout: paper
+title: "Functional and antigenic constraints on the Nipah virus fusion protein"
+date: "2025-10-15"
+authors: 
+    - "Brendan B Larsen"
+    - "Sheri Harari"
+    - "Risako Gen"
+    - "Cameron Stewart"
+    - "David Veesler"
+    - "Jesse D Bloom"
+journal: "bioRxiv"
+doi: "10.1101/2025.10.15.682664"
+link: "https://doi.org/10.1101/2025.10.15.682664"
+image: "/assets/papers/2025_larsen_f.jpg"
+keywords:
+    - "Nipah"
+    - "Deep mutational scanning"
+    - "Pseudovirus"
+selected: true
+---
+
+## 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 non-replicative 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 varies among antibodies. Our measurements of mutational effects on Nipah virus F predict the ability of the antibodies to neutralize the related Hendra virus. Overall, our work defines the functional and antigenic constraints on the F protein from an important zoonotic virus.
+
+## Interactive visualizations
+The results described in this paper can be interactively visualized at [https://dms-vep.org/Nipah_Malaysia_F_DMS/](https://dms-vep.org/Nipah_Malaysia_F_DMS/)
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