【摘要】：為設計大腸桿菌外膜蛋白OmpC的表位多肽重組疫苗,進一步提高OmpC蛋白的免疫效果,通過生物信息學軟件對OmpC蛋白的進化關系、高級結構與細胞表位進行分析。結果表明,大腸桿菌、沙門傷寒菌、肺炎克雷伯菌,這3種細菌具有較高同源性,OmpC蛋白可能對這3種菌株的感染起到交叉免疫保護作用。OmpC為親水性蛋白,1~21位氨基酸為信號肽位置,無跨膜結構并定位于細胞膜外;OmpC二級結構中含無規(guī)則卷曲43.05%,a-螺旋16.08%,β-轉角0%,β-片層40.87%。OmpC蛋白可能存在5個優(yōu)勢B細胞表位,1個CTL表位,1個Th細胞表位;并重組拼接獲得抗原性較好的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.
【作者單位】： 陜西理工大學中德天然產物研究所;陜西省天麻山茱萸工程技術研究中心;漢中市食品藥品檢驗檢測中心;
【基金】：陜西省農業(yè)科技創(chuàng)新與攻關項目(2016NY-088) 陜西理工大學校級科研項目(SLGKY16-13)
【分類號】：S852.4;S852.612

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