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

摘要

为设计大肠杆菌外膜蛋白OmpC的袁位多肽重组疫苗,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％,3-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.%In order to improve the immune effect of OmpC (outer membrane protein C) protein,the recombinant vaccine of Escherichia coli OmpC epitope polypeptide was designed.By bioinformatic software,the evolution relationship,advanced structure and cell epitopes of OmpC protein were analyzed.The results showed that the OmpC protein sequences of Escherichia coli,Salmonella,Klebsiella pneumoniae,had high homology,and OmpC antibodies might play a cross immune protective effect for these strains.OmpC was a hydrophilic protein,1 ～ 21 amino acids of OmpC was signal peptide sequence,and had not transmembrane structure being located outside the cell membrane.The OmpC secondary structure contained 43.05％ of random coil,16.08％ of alpha helix,0％ of beta turn,and 40.87％ of extended strand,respectively.OmpC might have 5 B-cell epitopes,1 CTL epitopes,and 1 Th epitopes,and OmpC protein epitope vaccine with good immunogenicity was obtained by recombinant splicing.