Efficacy of HIV Antibodies: Why Two Arms are Better than One
This event is part of the Biophysics Seminars. 12:30PM.
One important pathway used to mount an effective immune response against pathogens begins when antibodies tightly bind to invading particles. IgG antibodies usually accomplish this by simultaneously binding two antigen-binding arms (Fabs) if one Fab dissociates, IgGs can remain attached through the second arm, allowing the Fab to quickly reassociate. HIV foils this strategy by only having a few highly-separated Envelope spikes (Envs) on its surface for IgGs to bind. This forces antibodies to bind monovalently, causing IgGs to rapidly dissociate which mitigates the immune response. To counter this strategy, we explore the efficacies of an array of synthetic antibodies that vary in size and flexibility. We create a model that translates the geometry of each antibody into its neutralization potency and utilize it to theoretically design an optimal bivalent antibody to target HIV.