MENINGVAX / STRUCTURAL VACCINOLOGY / 018
Antigen Engineering
Applying protein structure, molecular diversity, and immunological evidence to the design of meningococcal vaccine antigens.
01 / RATIONAL ANTIGEN DESIGN
Engineering protective protein targets
Antigen engineering explores how changes to a protein's sequence or structure influence stability, epitope presentation, immunogenicity, and recognition across pathogen variants.
Sequence diversity
Determine whether antigen variants differ at immune-recognition sites.
Structural stability
Investigate protein folding, thermal stability, and preservation of protective epitopes.
Functional validation
Test whether engineered proteins elicit functional immune responses.
02 / CASE STUDY
Factor H-binding protein
Meningococcal factor H-binding protein (fHbp) helps the bacterium recruit human factor H, a regulator of complement activation. It is also a protective antigen used in licensed MenB vaccines.
Research has explored altered fHbp structures to improve stability or broaden antibody recognition. Promising laboratory findings do not by themselves establish clinical effectiveness.
Broader recognition without losing function
Structural modifications must preserve biologically relevant epitopes while accommodating sequence variation. Effects on immunogenicity require empirical testing.
Peer-reviewed references
- A meningococcal vaccine antigen engineered to increase thermal stability and stabilize protective epitopes. PubMed ↗
- Bactericidal antibody responses induced by meningococcal recombinant chimeric factor H-binding protein vaccines. PubMed ↗
- Structural characterization of a cross-protective natural chimera of factor H-binding protein. PubMed ↗