An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines

作者：Abdelhameed Ali Saber; Morris Gordon A; Adams Gary G; Rowe Arthur J; Laloux Olivier; Cerny Louis; Bonnier Benjamin; Duvivier Pierre; Conrath Karel; Lenfant Christophe; Harding Stephen E^*

来源：Carbohydrate Polymers, 2012, 90(4): 1831-1835.

DOI：10.1016/j.carbpol.2012.07.032

• Analytical ultracentrifugation
• Hydrodynamics
• Solution conformation

Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (similar to 86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio similar to 3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines.

• 出版日期2012-11-6