Allison C. Rice-ficht

Biography

Rice-Ficht received her Bachelor of Science from Auburn University and her doctorate from Vanderbilt University in 1980 investigating mechanisms of viral infection. In post-doctoral work at the University of Iowa she developed a keen interest in tropical diseases and uncovered the molecular basis of infection by the African sleeping sickness parasite, Trypanosoma brucei. Since 1984, Rice-Ficht has been a member of the faculty of the Texas A&M University Health Science Center continuing her interest in tropical disease and vaccine development. These studies unexpectedly revealed a natural capsule produced by parasitic worms that could be used for timed-release of vaccines and drugs. Rice-Ficht has engineered this capsule or particle with the ultimate goal of creating a needle-free “pocket vaccine” delivery system for the delivery of virtually any vaccine. The Rice-Ficht laboratory currently uses micro and nanoparticles for timed release of vaccines, producing a continual boosting effect and enhanced vaccination. This technology has been applied to the production of vaccines for brucellosis, tuberculosis and Q fever through funding from the National Institutes of Health, the Department of Defense and the Gates Foundation. Since 2002, Rice-Ficht has served as the director for the Center for Microencapsulation and Drug Delivery, a group of life scientists and engineers pioneering sustained and targeted delivery of vaccines and pharmaceuticals. She also serves as associate vice president for research of the Texas A&M Health Science Center.

Research Interest

Studies in the Rice-Ficht lab are currently focused on the use of unique biomaterials for controlled release of live and subunit vaccines. Our focus is currently directed to the production of vaccines against human Brucellosisand Q fever, but will be applied to the storage and delivery of other vaccines. A study of specific immune mechanisms and potentiation through controlled releases is underway. Another focus is the study of alpha crystalline structure and function. These unique proteins protect against thermal insult and modulate folding and activity of other proteins