α-β-α 三明治构象的完整性对于新型佐剂 TFPR1 保持其佐剂活性至关重要。
The Integrity of α-β-α Sandwich Conformation Is Essential for a Novel Adjuvant TFPR1 to Maintain Its Adjuvanticity.
机构信息
Beijing Institute of Microbiology and Epidemiology, Anhui Medical University, Hefei 230032, China.
State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China.
出版信息
Biomolecules. 2019 Dec 12;9(12):869. doi: 10.3390/biom9120869.
TFPR1 is a novel peptide vaccine adjuvant we recently discovered. To define the structural basis and optimize its application as an adjuvant, we designed three different truncated fragments that have removed dominant B epitopes on TFPR1, and evaluated their capacity to activate bone marrow-derived dendritic cells and their adjuvanticity. Results demonstrated that the integrity of an α-β-α sandwich conformation is essential for TFPR1 to maintain its immunologic activity and adjuvanticity. We obtained a functional truncated fragment TFPR-ta ranging from 40-168 aa of triflin that has similar adjuvanticity as TFPR1 but with 2-log fold lower immunogenicity. These results demonstrated a novel approach to evaluate and improve the activity of protein-based vaccine adjuvant.
TFPR1 是我们最近发现的一种新型肽疫苗佐剂。为了确定其结构基础并优化其作为佐剂的应用，我们设计了三个不同的截断片段，这些片段去除了 TFPR1 上的主要 B 表位，并评估了它们激活骨髓来源树突状细胞的能力及其佐剂活性。结果表明，α-β-α 三明治构象的完整性对于 TFPR1 维持其免疫活性和佐剂活性至关重要。我们获得了一个功能截断片段 TFPR-ta，它来自三肽重复蛋白 1 的 40-168 个氨基酸，具有与 TFPR1 相似的佐剂活性，但免疫原性低 2 个对数倍。这些结果为评估和改善基于蛋白质的疫苗佐剂的活性提供了一种新方法。
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