“Our research seeks to determine the relationship between antibody paratope, antigenic epitope and antibody function in the human immune response to vaccination and infection.”

Traditional approaches to vaccine development have proven ineffective for several important diseases. Contemporary vaccine design strategies for these diseases have adopted a “component” or “subunit” approach in which important immunogenic molecules associated with the infectious agent are present in vaccine formulations in place of the killed or attenuated agents more traditionally utilized. The effective design of such vaccines requires an in-depth understanding of the interactions between individual antibody binding domains (paratopes) and the region of the antigen to which they bind (epitope), as well as a determination of which paratope/ epitope interactions are effective in neutralizing the infecting agent.

Dr. Reason’s research seeks to define these interactions directly in humans by first defining the antibody repertoire that arises in response to vaccination or infection, and then by using these reagents to define the “epitopic repertoire” for the antigen as seen by the human host. The human monoclonal antibodies generated by this approach are then individually assayed to determine their efficacy in killing or neutralizing the infectious agent. Together this information identifies the epitope or epitopes that must be present in order for a vaccine to be effective, and in some cases reveals the mechanism by which efficacy is achieved.

Dr. Reason’s group has applied this approach to several serotypes of Streptococcus pneumoniae, to soluble toxins from Diphtheria and Anthrax, and to surface proteins associated with Neisseria meningitidis. Dr. Reason’s findings have provided significant new information that would not have been obtainable using more traditional techniques of polyclonal serology and may be useful in guiding future subunit vaccine design and development.

Revised: Friday, April 17, 2020 4:14 PM


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