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 Validations
Binding Validation by Biolayer Interferometry
To validate our DMS binding measurements, we tested binding affinity by biolayer interferometry. Notebook analyzing biolayer interferometry data and plotting 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
Analysis Notebooks
Notebook analyzing receptor binding from filtered data. Make figures for manuscript using python and altair.
Raw Data
These data have not been filtered. They are the raw output from dms-vep-pipeline-3. For filtered .csv files, click here
Individual receptor binding selection files
Averaged effects of RBP mutations on bEFNB2 binding across replicates
Averaged effects of RBP mutations on bEFNB3 binding across replicates