I am a molecular biologist and biochemist with more than 20 years of experience in Neisseria vaccine development, protein engineering, and structural vaccinology. My research program applies structural and mechanistic insights to the design of next-generation vaccine antigens targeting bacterial pathogens.
A major focus of our work is the engineering of meningococcal Factor H binding protein (FHbp) vaccine antigens through the structural decoupling of antigen immunogenicity from human complement Factor H binding. Using this approach, we have developed engineered antigens that elicit enhanced protective antibody responses in human-relevant models and have advanced to evaluation in two Phase 2 clinical trials.
Our laboratory integrates structural biology, immunology, and biochemistry to define the molecular basis of protective immunity. We use approaches such as X-ray crystallography to characterize protective epitopes in complex with antibody Fab fragments, providing mechanistic insight into cooperative antibody-mediated immune responses.
We have extended this structural framework to Neisseria gonorrhoeae, where we characterized gonococcal lipooligosaccharide (LOS) bound to a monoclonal antibody and identified a minimal saccharide vaccine candidate. In parallel, we engineer native outer membrane vesicle (NOMV) vaccines that display optimized antigens in their native membrane context. This platform has demonstrated cross-protective potential against both meningococci and gonococci and supports the development of multi-antigen vaccines targeting antimicrobial-resistant pathogens.