Erin Swanson

Immunoglobulins (Ig) are essential components of the adaptive immune system. Through affinity maturation and class switching (from IgM or IgD to IgG, IgE, or IgA), antibodies evolve to bind antigens with higher affinity, triggering a variety of effector mechanisms to clear pathogens. Some isotypes, including IgA and IgM in humans, can be assembled into polymeric (p) Igs, which contain two to six Ig monomers and up to one joining chain and one secretory component. Each monomer is related through unique geometric relationships. To investigate how Ig polymeric state and geometry influences pIg-dependent pathogen neutralization, I am developing a library of pIgs, integrating the same antigen binding domains into different pIg scaffolds (both endogenous and engineered). I test this library in vitro against various pathogens (Influenza A and Clostridioides difficile) and use structural biochemistry to uncover correlations between Ig sequence, geometry, function, and potency. Ultimately, these trends will guide future rational design of novel pIg therapeutics targeting infection disease.