梅毒螺旋体黏附蛋白生物信息学分析  

Bioinformatic analysis of adhesion proteins of Treponema pallidum

作　　者：郭宁远 李思佳 李威威 赵思思 吴移谋[1] GUO Ning-yuan;LI Si-jia;LI Wei-wei;ZHAO Si-si;WU Yi-mou(Hunan Provincial Key Laboratory of Special Pathogen Prevention and Control,Institute of Pathogen Biology,University of South China,Hunan 421000,China)

机构地区：[1]南华大学病原生物学研究所特殊病原体防控湖南省重点实验室,湖南421000

出　　处：《中国卫生检验杂志》2023年第4期421-425,共5页Chinese Journal of Health Laboratory Technology

摘　　要：目的 对梅毒螺旋体(Tp)7种黏附蛋白作更进一步的生物信息学分析,为其在Tp致病过程中的机制研究提供理论依据。方法 通过使用NCBI、BLAST、CDD、BioEdit、ExPASy、SignalP、TMHMM、NetMHC II pan 3.2等生物信息学分析方法,分析7种黏附蛋白的一般性质、信号肽、糖基化位点、磷酸化位点及抗原表位等。结果 分析预测了Tp中7种黏附蛋白一般性质,7种黏附蛋白皆为亲水性蛋白,除Tp0155、Tp0750外,均具有跨膜结构域,除Tp0483外,均含有信号肽,除Tp0435和Tp0483外,其余蛋白均具有糖基化位点,7种黏附蛋白均含多个磷酸化位点以及B细胞、T细胞表位。结论 7种黏附蛋白在Tp入侵宿主时,极有可能降解宿主细胞外基质中的成分继而穿透基底膜并且损伤宿主细胞,从而有利于Tp在宿主体内的侵袭和播散。Objective This study aims to further bioinformatics analysis of 7 adhesion proteins of Treponema pallidum(Tp), so as to provide theoretical basis for the study of the pathogenic mechanism of Tp. Methods NCBI, BLAST, CDD, BioEdit, ExPASy, SignalP, TMHMM, NetMHC II pan 3.2 and other bioinformatics methods were used to analyze the general properties, signal peptides, glycosylation sites, phosphorylation sites and epitopes of seven adhesive proteins. Results The general properties of seven adhesion proteins in Tp were analyzed. All the seven adhesion proteins were hydrophilic proteins. Except Tp0155 and Tp0750, they all had transmembrane domains;except Tp0483, they all contained signal peptides;except Tp0435 and Tp0483, the other proteins all had glycoylation sites. All the 7 adhesion proteins contained multiple phosphorylation sites and B cell and T cell epitopes. Conclusion The seven adhesive proteins are highly likely to degrade the components in the extracellular matrix of the host and then penetrate the basement membrane and damage the host cells, which facilitates the invasion and dissemination of Tp in the host.

关 键 词：梅毒螺旋体 黏附蛋白 侵袭 

分 类 号：R446[医药卫生—诊断学]