FAB Antibody bound to Meningococcal fHbp Volumetric


3D printed protein models of a FAB Antibody bound to Meningococcal fHbp (Ribbon) . This model is designed to pair with the academic publication, Crystal structure reveals vaccine elicited
bactericidal human antibody targeting a conserved epitope on meningococcal fHbp. (LINK )

The chains of these protein models are colored yellow and green for the antibody FAB fragments, and cyan and light blue for the fHbp. The chains of each protein are colored to enhance understanding of the protein structure by coloring the alpha helices, beta sheets and colors decreasing intensities of color saturation. To highlight the binding residues found in the research publication, we have colored each amino acid by atom type.




Data obtained recently in the United Kingdom following a nationwide infant immunization program against serogroup B Neisseria meningitidis (MenB) reported >80% 4CMenB vaccine-mediated protection. Factor H-binding protein (fHbp) is a meningococcal virulence factor and a component of two new MenB vaccines. Here, we investigated the structural bases underlying the fHbp-dependent protective antibody response in humans, which might inform future antigen design efforts. We present the co-crystal structure of a human antibody Fab targeting fHbp. The vaccine-elicited Fab 1A12 is cross-reactive and targets an epitope highly conserved across the repertoire of three naturally occurring fHbp variants. The free Fab structure highlights conformational rearrangements occurring upon antigen binding. Importantly, 1A12 is bactericidal against MenB strains expressing fHbp from all three variants. Our results reveal important immunological features potentially contributing to the broad protection conferred by fHbp vaccination. Our studies fuel the rationale of presenting conserved protein epitopes when developing broadly protective vaccines.

PDB ID: 5O14z



Additional information

Weight 1 lbs
Dimensions 8 x 8 x 4 cm

Small, Medium, Large


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