Receptor Binding
To understand how mutations affect binding to ephrin receptors, we performed selections on our pseudovirus libraries with soluble bat ephrin-B2 and ephrin-B3. Neutralization of pseudovirus variants serves as a proxy for receptor binding. Neutralization curves were fit with polyclonal.
Pseudoviruses expressing unmutated Nipah virus receptor binding and fusion proteins were neutralized by soluble bat ephrin receptors.
Individual Receptor Binding Selections
Individual antibody selection model fitting notebooks
Average Receptor Binding
These notebooks average effects of mutations on receptor binding across libraries and replicate selections.
Comprehensive Receptor Binding Heatmaps
Additional control over filtering parameters. Users can adjust different parameters to filter the heatmap data. These provide more information and control compared to the final filtered heatmaps provided on the heatmaps page.
Binding Correlations
Binding Validation by Neutralization
We also tested neutralization of individual mutations expressed on pseudoviruses with soluble bat ephrin-B2 (monomeric) or bat ephrin-B3 (dimeric). Individual mutations affect neutralizing potency by soluble receptor. Binding validations notebook
Binding Validation by Neutralization
We also tested neutralization of individual mutations expressed on pseudoviruses with soluble bat ephrin-B2 (monomeric) or bat ephrin-B3 (dimeric). Individual mutations affect neutralizing potency by soluble receptor. Binding validations notebook