Bloom Lab Blog

In a new study we posted on bioRxiv today, we measured how all mutations to the rabies virus glycoprotein (G) affect cell entry and antibody neutralization. This study sheds light on mutational constraints on class III viral fusion proteins, suggests ways to stabilize G for vaccine antigens, and quantifies the robustness of antibodies (including ones being used or developed for clinical use) to rabies genetic variation.

I've updated the SARS-CoV-2 RBD antibody escape calculator with new yeast-display deep mutational scanning data from Yunlong Cao's group. My interpretation: the antigenic evolution of the RBD is currently constrained by the pleiotropic effects of mutations on 1:1 RBD-ACE2 affinity, up-down RBD positioning in the context of full spike, and antibody neutralization.

In a paper just published in Journal of Virology, we describe a new sequencing-based neutralization assay that dramatically increases the scale at which it is possible to measure how sera or antibodies neutralize different influenza virus strains.

In a new study, we have measured how all mutations to the hemagglutinin (HA) of clade 2.3.4.4b H5 influenza affect molecular phenotypes relevant to pandemic risk. The data can be interactively visualized at https://dms-vep.org/Flu_H5_American-Wigeon_South-Carolina_2021-H5N1_DMS/