An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines
An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines
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DOI：
10.1016/j.carbpol.2012.07.032
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发表时间：
2012-11-06
影响因子：
11.2
通讯作者：
Harding, Stephen E.
中科院分区：
文献类型：
--
作者：
Abdelhameed, Ali Saber;Morris, Gordon A.;Harding, Stephen E.
破伤风类毒素蛋白在低聚状态和流体动力学（低分辨率）形状方面具有特征，这是其在糖结合疫苗中使用的重要参数。通过对分析式超离心沉降速度和沉降平衡分析，破伤风类毒素蛋白在溶液中主要为单体（约86%），约14%为二聚体。相对比例不随浓度的变化而明显变化，表明两组分不处于可逆平衡状态。基于高精度粘度法的流体动力学溶液构象研究，结合沉降数据表明，蛋白质在溶液中的构象略有延长，长径比接近3。这种不对称结构比球状结构具有更大的与多糖结合的表面积，支持其作为糖结合疫苗结合蛋白的普遍选择。(C) 2012 Elsevier Ltd.版权所有。
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. (C) 2012 Elsevier Ltd. All rights reserved.