乙肝表面抗原-CD40L胞外段融合蛋白的设计和生物活性预测

Design of HBsAg-ecdCD40L fusion protein and prediction of its biological characteristics

目的:探讨乙肝表面抗原-CD40L胞外段融合蛋白设计的合理性。方法:应用Gene Constructionkit2.5、DNAStar软件和www.expasy.org网站提供的分析方案分析重组体的开放读框以及融合蛋白的柔性、亲水性、抗原性、表位等性质,并作了二级结构模拟分析。结果:重组体CMV启动子下游有完整的目的基因ORF,融合蛋白二级结构水平未出现新的抗原性及表位,亲水性无改变,Linker部位抗原性低,呈中性且柔性高,不影响两端的蛋白质二级结构及融合蛋白空间构象。结论:重组体设计合理,融合蛋白很大可能保留了乙肝表面抗原和CD40L胞外段的生物学活性,为进一步研究提供了理论依据。

Objective： To explore the reasonability of the design of HBsAg-ecdCD40L fusionprotein. Methods： Using sequence analysis software and protocols prescribed on website www.expasy.com the open reading frame of the recombinant plasmid and the flexibility,hydrophilicity,antigenicity and epitope of recombinant HBsAg-ecdCD40L were analyzedand the secondary structure of HBsAg-ecdCD40L fusion protein was analyzed, too. Resuits： The fusion protein had correct domains of ttBsAg and ecdCD40L. The linker had low antigencity and high flexibility and might not influence the secondary structure of the fusion protein. Conclusion： The design of the fusion protein is reasonable. It Keeps the maximum biological activities of HBsAg and ecdCD40L.