鹦鹉热衣原体MIP蛋白生物信息学分析

Bioinformatics Analysis of Chlamydia psittaci MIP Protein

为初步了解鹦鹉热衣原体(Chlamydia psittaci,Cps)巨噬细胞感染增强蛋白(macrophage infection potentiator,MIP)的生物学特征。本研究从美国国家生物技术信息中心(national center for biotechnology infor mation,NCBI)数据库中检索并下载全部Cps菌株的MIP基因序列,运用生物信息学软件分析Cps不同菌株间MIP基因的同源性,MIP蛋白的氨基酸序列、理化性质、跨膜区、信号肽、空间结构以及抗原表位。结果显示:MIP基因在Cps不同菌株间的同源性为98.96%~99.87%。生物信息学软件预测MIP蛋白为一种性质不稳定、弱酸性的亲水蛋白;该蛋白无跨膜区和信号肽;α螺旋与β转角是其主要结构特征;该蛋白含有5个优势B细胞抗原表位,2个优势T细胞抗原表位。Cps MIP为弱酸性、亲水性且不参与物质运输的蛋白,具有优势B、T淋巴细胞抗原表位,是良好的潜在疫苗。

To investigate the biological characteristics of Macrophage infection potentiator(MIP)of Chlamydia psittaci.The MIP gene sequences of all C.psittaci strains were retrieved and downloaded from the national center for biotechnology information(NCBI).The homology of MIP genes was compared among different C.psittacis strains,and the amino acid sequence,physicochemical properties,transmembrane region,signal peptide,spatial structure and antigenic epitopes of MIP protein were analyzed with bioinformatics softwares.The results showed:the homology of MIP gene among different C.psittaci strains was 98.96%~99.87%.C.psittaci MIP protein was an unstable and weak acidic hydrophilic protein,had no transmembrane domain and signal peptide andα-helix andβ-turn were its major structural features.There were five dominant B cell antigen epitopes and two dominant T cell antigen epitopes in C.psittaci MIP protein.C.psittaci MIP is a weakly acidic,hydrophilic protein which does not participate in the transport of substances,and has T and B cell antigen epitopes indicate it can act as a good potential vaccine candidate.