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首页> 外文期刊>Vaccine >Increasing the humoral immunogenic properties of the HIV-1 Tat protein using a ligand-stabilizing strategy.
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Increasing the humoral immunogenic properties of the HIV-1 Tat protein using a ligand-stabilizing strategy.

机译：使用配体稳定策略提高HIV-1 Tat蛋白的体液免疫原性。

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摘要

Tat is regarded as an attractive target for the development of an AIDS vaccine. However, works suggest that Tat is a poorly immunogenic protein and therefore we attempted to increase its immunogenic potency. As we observed that Tat is highly sensitive to enzymatic degradation in vitro we tried to make it less susceptible to proteolysis using ligands. We complexed Tat101 with various sulfated sugars and observed that some of these ligands made the protein more resistant to proteolysis and more immunogenic. In a more thorough study, we observed that a low-molecular-weight heparin fragment, called Hep6000, altered both the cell-binding capacity and transactivating activity of Tat101, suggesting that this sulfated polysaccharide can make the protein less toxic. Sera raised against Tat101 and Tat101/Hep6000 similarly bound mainly to the N-terminal region of the protein, indicating that formation of the complex does not alter the B-cell immunodominant region. Anti-Tat101/Hep6000 antisera neutralized the transactivating activity of Tat101 more efficiently than anti-Tat101 antisera. Altogether, these results indicate that stabilization of Tat101 using sulfated sugars increases its immunogenicity and might be of value in increasing its vaccine efficacy.
机译：Tat被认为是开发AIDS疫苗的诱人目标。但是，研究表明Tat是一种免疫原性较差的蛋白质，因此我们试图提高其免疫原性。正如我们观察到的，Tat对体外酶促降解高度敏感，我们试图使其不易受配体蛋白水解的影响。我们将Tat101与各种硫酸化的糖复合，并观察到这些配体中的一些使蛋白质对蛋白水解的抵抗力和免疫原性更高。在更深入的研究中，我们观察到称为Hep6000的低分子量肝素片段改变了Tat101的细胞结合能力和反式激活活性，表明这种硫酸化多糖可以使蛋白质的毒性降低。针对Tat101和Tat101 / Hep6000产生的血清类似地主要结合至蛋白质的N端区域，表明复合物的形成不会改变B细胞免疫显性区域。抗Tat101 / Hep6000抗血清比抗Tat101抗血清更有效地中和了Tat101的反式激活活性。总之，这些结果表明使用硫酸化糖稳定Tat101可以提高其免疫原性，并可能在提高其疫苗效力方面具有价值。

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