大肠杆菌外膜蛋白OmpC的生物信息学分析及表位多肽疫苗的重组预测
发布时间：2018-12-23 20:53
【摘要】：为设计大肠杆菌外膜蛋白OmpC的表位多肽重组疫苗,进一步提高OmpC蛋白的免疫效果,通过生物信息学软件对OmpC蛋白的进化关系、高级结构与细胞表位进行分析。结果表明,大肠杆菌、沙门伤寒菌、肺炎克雷伯菌,这3种细菌具有较高同源性,OmpC蛋白可能对这3种菌株的感染起到交叉免疫保护作用。OmpC为亲水性蛋白,1~21位氨基酸为信号肽位置,无跨膜结构并定位于细胞膜外;OmpC二级结构中含无规则卷曲43.05%,a-螺旋16.08%,β-转角0%,β-片层40.87%。OmpC蛋白可能存在5个优势B细胞表位,1个CTL表位,1个Th细胞表位;并重组拼接获得抗原性较好的OmpC蛋白表位多肽。
[Abstract]:In order to design the recombinant vaccine of epitope polypeptide of Escherichia coli outer membrane protein OmpC and further improve the immune effect of OmpC protein, the evolutionary relationship, advanced structure and cell epitope of OmpC protein were analyzed by bioinformatics software. The results showed that Escherichia coli, Salmonella typhimurium, Klebsiella pneumoniae had high homology, and OmpC protein might play a cross-immunological protective effect on the infection of these three strains. OmpC is a hydrophilic protein. (1) Amino acids at the 21 ~ (th) position are signal peptide positions, and have no transmembrane structure and are located outside the cell membrane; The secondary structure of OmpC contained irregular crimping 43.05ka-helix 16.08, 尾 -rotation angle 0. The 尾 -lamellar 40.87%.OmpC protein may have five dominant B cell epitopes, one CTL epitope and one Th cell epitope. OmpC epitope peptides with good antigenicity were obtained by recombinant splicing.
【作者单位】： 陕西理工大学中德天然产物研究所;陕西省天麻山茱萸工程技术研究中心;汉中市食品药品检验检测中心;
【基金】：陕西省农业科技创新与攻关项目(2016NY-088) 陕西理工大学校级科研项目(SLGKY16-13)
【分类号】：S852.4;S852.612
[Abstract]:In order to design the recombinant vaccine of epitope polypeptide of Escherichia coli outer membrane protein OmpC and further improve the immune effect of OmpC protein, the evolutionary relationship, advanced structure and cell epitope of OmpC protein were analyzed by bioinformatics software. The results showed that Escherichia coli, Salmonella typhimurium, Klebsiella pneumoniae had high homology, and OmpC protein might play a cross-immunological protective effect on the infection of these three strains. OmpC is a hydrophilic protein. (1) Amino acids at the 21 ~ (th) position are signal peptide positions, and have no transmembrane structure and are located outside the cell membrane; The secondary structure of OmpC contained irregular crimping 43.05ka-helix 16.08, 尾 -rotation angle 0. The 尾 -lamellar 40.87%.OmpC protein may have five dominant B cell epitopes, one CTL epitope and one Th cell epitope. OmpC epitope peptides with good antigenicity were obtained by recombinant splicing.
【作者单位】： 陕西理工大学中德天然产物研究所;陕西省天麻山茱萸工程技术研究中心;汉中市食品药品检验检测中心;
【基金】：陕西省农业科技创新与攻关项目(2016NY-088) 陕西理工大学校级科研项目(SLGKY16-13)
【分类号】：S852.4;S852.612
【相似文献】
相关期刊论文 前1条
1 刘曼;杨桂连;王春凤;刘琼;何佳雪;李颖;;鸡白痢沙门氏菌外膜蛋白C基因(OmpC)的克隆与表达[J];中国预防兽医学报;2009年02期
相关会议论文 前1条
1 贺聪;林崇韫;陈峰;毕英佐;谢青梅;;鸡白痢沙门氏菌外膜蛋白C(ompC)的原核表达[A];第四届第十次全国学术研讨会暨动物微生态企业发展战略论坛论文集（下册）[C];2010年
相关硕士学位论文 前1条
1 韩乐o，
本文编号：2390248
本文链接：https://www.wllwen.com/yixuelunwen/dongwuyixue/2390248.html
