research

Adaptive immune responses to infection

Current structural characterizations of antibody-antigen binding often only involve amino acid residues. Antigens rapidly evolve not only in their protein sequence, but also in their post-translational modifications including glycosylation. In addition, many pathogens including bacteria and fungi have glycan-based antigens. We aim to comprehensively map and characterize pathogen-specific and cross-reactive antibodies that involve binding to non-amino acid moieties to enhance current vaccine design efforts.

Protein engineering for immunotherapy and vaccine design

Vaccine immunogen design and antibody-based immunotherapy require rational protein engineering. By developing high-throughput biochemichal and molecular tools, we can accelerate protein design that have the desired biochemical and biophysical properties for immunotherapy. For example, we established a pipeline to rapidly identify prefusion-stabilizing mutations of membrane-bound and soluble SARS-CoV-2 spike protein to elicit protective, neutralizing RBD-directing antibodies. By searching large protein fitness landscapes, we can chart functional trajectories of evolving antigens.