PDF(Pubmed)
Abstract：
UNASSIGNED: The current in silico study was done to determine the primary biochemical features and immunogenic epitopes of Echinococcus granulosus glutathione S-transferase protein as a potential vaccine candidate.
UNASSIGNED: Several web tools were employed to predict physico-chemical properties, antigenicity, allergenicity, solubility, post-translational modification (PTM) sites, subcellular localization, signal peptide, transmembrane domain, secondary and tertiary structure followed by refinement and validations. In addition, B-cell epitopes were predicted and were screened using various web servers, while MHC-binding and CTL epitopes were predicted using IEDB and NetCTL servers, respectively.
UNASSIGNED: The protein had 219 residues with a molecular weight of 25.55 kDa and alkaline isoelectric pH (7.5). This protein was stable, thermo-tolerant (aliphatic index: 78.04) and hydrophilic (GRAVY: -0.440). The predicted antigenicity scores were low and the protein was nonallergenic in nature. There were no transmembrane domain and signal peptide in the sequence. Moreover, several B-cell, MHC-binding and CTL epitopes were found in the EgGST protein, which could be further used in multi-epitope vaccines.
UNASSIGNED: Further studies are needed on the development of vaccines in vivo using EgGST alone or in combination with other antigens in the future.
UNASSIGNED: Several web tools were employed to predict physico-chemical properties, antigenicity, allergenicity, solubility, post-translational modification (PTM) sites, subcellular localization, signal peptide, transmembrane domain, secondary and tertiary structure followed by refinement and validations. In addition, B-cell epitopes were predicted and were screened using various web servers, while MHC-binding and CTL epitopes were predicted using IEDB and NetCTL servers, respectively.
UNASSIGNED: The protein had 219 residues with a molecular weight of 25.55 kDa and alkaline isoelectric pH (7.5). This protein was stable, thermo-tolerant (aliphatic index: 78.04) and hydrophilic (GRAVY: -0.440). The predicted antigenicity scores were low and the protein was nonallergenic in nature. There were no transmembrane domain and signal peptide in the sequence. Moreover, several B-cell, MHC-binding and CTL epitopes were found in the EgGST protein, which could be further used in multi-epitope vaccines.
UNASSIGNED: Further studies are needed on the development of vaccines in vivo using EgGST alone or in combination with other antigens in the future.
摘要：
■进行了当前的计算机研究，以确定细粒棘球蚴谷胱甘肽S-转移酶蛋白作为潜在疫苗候选物的主要生化特征和免疫原性表位。
■采用了几种网络工具来预测物理化学性质，抗原性,变应原性,溶解度，翻译后修饰(PTM)位点,亚细胞定位，信号肽，跨膜结构域，二级和三级结构，然后进行细化和验证。此外,对B细胞表位进行了预测，并使用各种网络服务器进行了筛选，虽然MHC结合和CTL表位是使用IEDB和NetCTL服务器预测的，分别。
■该蛋白质具有219个残基，分子量为25.55kDa，具有碱性等电pH（7.5）。这种蛋白质是稳定的,耐热性（脂肪指数：78.04）和亲水性（GRAVY：-0.440）。预测的抗原性得分较低，并且该蛋白质本质上是非过敏性的。序列中没有跨膜结构域和信号肽。此外，几个B细胞，在EgGST蛋白中发现了MHC结合和CTL表位，可进一步用于多表位疫苗。
■未来需要进一步研究单独使用EgGST或与其他抗原联合使用的体内疫苗的开发。
■采用了几种网络工具来预测物理化学性质，抗原性,变应原性,溶解度，翻译后修饰(PTM)位点,亚细胞定位，信号肽，跨膜结构域，二级和三级结构，然后进行细化和验证。此外,对B细胞表位进行了预测，并使用各种网络服务器进行了筛选，虽然MHC结合和CTL表位是使用IEDB和NetCTL服务器预测的，分别。
■该蛋白质具有219个残基，分子量为25.55kDa，具有碱性等电pH（7.5）。这种蛋白质是稳定的,耐热性（脂肪指数：78.04）和亲水性（GRAVY：-0.440）。预测的抗原性得分较低，并且该蛋白质本质上是非过敏性的。序列中没有跨膜结构域和信号肽。此外，几个B细胞，在EgGST蛋白中发现了MHC结合和CTL表位，可进一步用于多表位疫苗。
■未来需要进一步研究单独使用EgGST或与其他抗原联合使用的体内疫苗的开发。
