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目的探明甲壳类动物各种过敏原之间是否存在相似性,以期深入研究甲壳类食品过敏原的构效关系。方法应用生物信息学方法,分析预测了甲壳类动物的4种过敏原—原肌球蛋白(TM)、精氨酸激酶(AK)、肌球蛋白轻链(MLC)和肌质钙结合蛋白(SCP)的二级结构、亲水性、可塑性、抗原性、表面可及性、线性抗原表位和三维结构等。结果 TM为超螺旋结构,而AK、MLC和SCP均为复合蛋白,含有较多的Turn和Coil结构;TM、AK、MLC和SCP 4种过敏原的亲水性区域均在60%以上,可塑性区域约为50%,抗原性区域均在60%以上。TM、AK、MLC和SCP分别有11、10、4和4个线性抗原表位。TM、AK、MLC和SCP的三维结构建模结果与相应的二级结构预测结果一致,基本能够反映此4种过敏原的空间构象。结论通过生物信息学方法分析,同时获得了甲壳类动物4种过敏原TM、AK、MLC和SCP的分子特征、抗原表位及部分三维结构,可望为进一步采用实验方法研究其构效关系奠定理论基础。
Objective To find out whether there is a similarity between the various allergens of crustaceans in order to further study the structure-activity relationship of crustacean food allergens. Methods Using bioinformatics methods, the four allergens - tropomyosin (TM), arginine kinase (AK), myosin light chain (MLC) and sarcoplasmic reticulum calcium binding protein SCP) secondary structure, hydrophilicity, plasticity, antigenicity, surface accessibility, linear epitopes and three-dimensional structure. Results TM was a supercoiled structure, while AK, MLC and SCP were all complex proteins with more Turn and Coil structures. The hydrophilic regions of TM, AK, MLC and SCP allergens were over 60% The area is about 50%, antigenic areas are more than 60%. TM, AK, MLC and SCP have 11, 10, 4 and 4 linear epitopes respectively. The three-dimensional structure modeling results of TM, AK, MLC and SCP are in good agreement with the corresponding secondary structure prediction results, which basically reflect the spatial conformation of the four allergens. Conclusions The molecular characteristics, antigenic epitopes and some three-dimensional structures of four allergens TM, AK, MLC and SCP in crustaceans were obtained simultaneously by bioinformatics analysis. It is expected that the structure-activity relationship of the four allergens TM, AK, MLC and SCP will be further studied by using experimental methods Theoretical basis.