Hydrophobic moeties in recombinant proteins are crucial to generate efficient saponin-based vaccine against Apicomplexan Babesia divergens
Hydrophobic moeties in recombinant proteins are crucial to generate efficient saponin-based vaccine against Apicomplexan Babesia divergens
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DOI：
10.1016/j.vaccine.2005.08.073
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发表时间：
2006-01-30
期刊：
影响因子：
5.5
通讯作者：
Précigout, E
中科院分区：
文献类型：
--
作者：
Delbecq, S;Hadj-Kaddour, K;Précigout, E
在整个欧洲，牛巴贝斯虫病主要由分歧巴贝斯虫引起，这是一种通过蜱叮咬传播的顶复门寄生虫。B，分歧裂殖子的红细胞内发育导致溶血性贫血，牛巴贝虫病是造成农业企业经济损失的原因。最近描述了一种基于裂殖子表面蛋白Bd37和皂苷基拉的完全有效的重组疫苗。在本研究中，我们确定了由Bd37重组蛋白引起的保护性免疫与蛋白中疏水残基的存在有关。利用Bd37和Lis的多聚融合技术，在体外无细胞表达条件下，成功地表达了含有疏水序列的重组蛋白，不需要GST融合。我们使用不同的疏水序列和不同的重组Bd37蛋白来证明抗原疏水性影响免疫系统，将低效蛋白质转化为100%保护性疫苗。本文还讨论了有关疏水效应的假说及其在其他寄生虫疫苗中的应用前景。(c)2005爱思唯尔有限公司保留所有权利。
Throughout Europe, bovine babesiosis is mainly caused by Babesia divergens, an Apicomplexan parasite transmitted by tick bites. The intra-erythrocytic development of B, divergens merozoites leads to haemolytic anaemia, and bovine babesiosis is responsible for economic losses in the agro-business industry. A totally efficient recombinant vaccine based on the merozoite surface protein Bd37 and saponin QuilA was recently described. In the present study we determined that protective immunity elicited by the Bd37 recombinant protein was related to the presence of hydrophobic residues in the protein. Using polymeric fusion of Bd37 as well Lis cell-free in vitro protein expression, we successfully expressed recombinant proteins containing hydrophobic sequences Without the need of GST fusion. We used different hydrophobic sequences and different recombinant Bd37 proteins to demonstrate that antigen hydrophobicity affects the immune system, turning an inefficient protein into a 100% protective vaccine. Sonic hypotheses about the hydrophobic effect and its potential application to other parasitic protozoa vaccine are also discussed. (c) 2005 Elsevier Ltd. All rights reserved.