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Rationally designed minimized TbpB confers broad protection against meningococcal infection
Epshita A Islam1, Jamie E Fegan2, Gregory B Cole1
1Department of Biochemistry, Temerty Faculty of Medicine, University of Toronto, Toronto, Canada.
Plos Pathogens
|August 10, 2026
Summary
Engineered a minimized Transferrin binding protein B (TbpB) variant, the "loopless C-lobe," to overcome antigenic variability. This novel immunogen elicits broad protection against diverse Neisseria meningitidis strains, advancing vaccine development.
Area of Science:
- Vaccinology
- Structural Biology
- Microbiology
Background:
- Transferrin binding protein B (TbpB) is a vaccine candidate against pathogenic Neisseria species.
- Antigenic variability of TbpB hinders the development of a broadly protective vaccine.
Purpose of the Study:
- To engineer a minimized TbpB variant (loopless C-lobe) as a broadly protective immunogen.
- To evaluate the structural integrity and immunogenic potential of the engineered TbpB variant.
Main Methods:
- Structure-informed antigen engineering to remove variable surface loops from TbpB's C-lobe.
- Structural characterization and stability studies.
- Murine immunization and challenge studies for N. meningitidis infection models.
Main Results:
- The loopless C-lobe demonstrated structural integrity and stability.
- Murine studies showed robust protective efficacy against N. meningitidis invasive infection and colonization.
- The loopless C-lobe elicited broader cross-protection than intact TbpB or native C-lobe.
Conclusions:
- Structure-informed antigen engineering can overcome TbpB's antigenic variability.
- The loopless C-lobe is a promising immunogen for developing broadly efficacious vaccines against Neisseria pathogens.