An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines
详细信息 查看全文
- 作者：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
- 关键词：Analytical ultracentrifugation ; Hydrodynamics ; Solution conformation
- 刊名：Carbohydrate Polymers
- 出版年：2012
- 出版时间：6 November, 2012
- 年：2012
- 卷：90
- 期：4
- 页码：1831-1835
- 全文大小：348 K
文摘
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.