Pathogenic bacteria of the genus Neisseria have a siderophore-independent iron-uptake system reliant on a direct interaction between the bacterial cell and human transferrin (hTf), a serum protein. In the meningococcus, this uptake system is dependent on two surface-exposed, transferrin-binding proteins (Tbps), TbpA and TbpB. TbpA is highly conserved among meningococcal strains, and is thought to be a porin-like integral protein that functions as a gated channel for the passage of iron into the periplasm. TbpB is more variable in size, lipidated and fully surface-exposed. Given its location on the cell surface, its role in pathogenicity and interstrain sequence conservation, TbpA is currently being regarded for inclusion in a meningococcal vaccine effective against all serogroups. This requires gaining knowledge of the ligand—receptor interactions. In the present study we have optimized a procedure for obtaining purified, functionally active recombinant TbpA at a level and stability necessary for the initiation of such studies.
Expression and purification of functional recombinant meningococcal transferrin-binding protein A
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Jonathan S. OAKHILL, Christopher L. JOANNOU, Susan K. BUCHANAN, Andrew R. GORRINGE, Robert W. EVANS; Expression and purification of functional recombinant meningococcal transferrin-binding protein A. Biochem J 15 June 2002; 364 (3): 613–616. doi: https://doi.org/10.1042/bj20020500
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