Bexsero, a new vaccine against Neisseria meningitidis serogroup B (MenB), is 
composed of 3 main recombinant proteins and an outer membrane vesicle component. 
One of the main bactericidal antigens, neisseria heparin binding antigen (NHBA), 
is present as a fusion protein with the accessory protein genome-derived 
neisserial antigen (GNA) 1030 to further increase its immunogenicity. The gene 
encoding for GNA1030 is present and highly conserved in all Neisseria strains, 
and although orthologs are present in numerous species, its biologic function is 
unknown. Native mass spectrometry was used to demonstrate that GNA1030 forms a 
homodimer associated with 2 molecules of ubiquinone-8 (Ub8), a cofactor mainly 
involved in the electron transport chain and with antioxidant properties. Disc 
diffusion assays on the wild-type and knockout mutant of GNA1030, in the 
presence of various compounds, suggested that GNA1030 is not involved in 
oxidative stress or electron chain transport per se, although it contributes to 
constitutive refilling of the inner membrane with Ub8. These studies shed light 
on an accessory protein present in Bexsero and reveal functional insights into 
the family of related proteins. On the basis of our findings, we propose to name 
the protein neisseria ubiquinone binding protein (NUbp).