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

Ali Saber Abdelhameed, Gordon A. Morris, Gary G. Adams, Arthur J. Rowe, Olivier Laloux, Louis Cerny, Benjamin Bonnier, Pierre Duvivier, Karel Conrath, Christophe Lenfant, Stephen E. Harding

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18 Citations (Scopus)


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 (∼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 ∼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.

Original languageEnglish
Pages (from-to)1831-1835
Number of pages5
JournalCarbohydrate Polymers
Issue number4
Early online date15 Jul 2012
Publication statusPublished - 6 Nov 2012
Externally publishedYes


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