We are broadly interested in how the molecular properties of viral proteins and antibodies constrain their evolution and co-evolution.
Viral proteins and antibodies acquire amino acid substitutions at a rate orders of magnitude above most eukaryotic proteins. These substitutions can have pleiotropic consequences on protein stability, folding, and function. Our lab is developing high-throughput evolution and phenotyping assays to determine how these properties, and trade-offs between them, constrain and potentiate the evolution of viral proteins and antibodies, and how this varies between distinct selection environments. These experimental platforms will enable us to (1) determine key constraints on protein evolution, (2) predict the emergence of new viral variants, and (3) design therapeutic strategies that are refractory to the development of resistance.