华支睾吸虫一氧化氮合酶相互作用蛋白基因的生物信息学分析

Bioinformatics analysis of nitric oxide synthase interacting protein gene from Clonorchis sinensis

目的分析和预测华支睾吸虫一氧化氮合酶相互作用蛋白(CsNOSIP)基因序列结构和功能特征及其编码蛋白的理化性质,预测该基因的生物学意义。方法利用生物信息学方法(Vector NTI、InterProScan、SignalP和SecretomeP等相关软件)对华支睾吸虫一氧化氮合酶相互作用蛋白基因及相应氨基酸序列的同源性、理化性质、保守结构域、信号肽、亲水性/疏水性、B细胞表位进行预测分析。结果华支睾吸虫一氧化氮合酶相互作用蛋白基因的开放阅读框包含867 bp,编码288个氨基酸,理论分子质量为35 Mr,等电点为9.16。SignalP和SecretomeP分析结果显示华支睾吸虫一氧化氮合酶相互作用蛋白为非经典途径分泌蛋白;InterProScan分析结果显示,华支睾吸虫一氧化氮合酶相互作用蛋白特征性结构域位于第45~76位,第211~267位和第1~289位氨基酸之间。在该基因的氨基酸序列中,共发现7个B细胞表位。结论利用生物信息学知识和各种分析软件对Cs NOSIP所编码的cDNA序列及理论蛋白质的理化性质、结构和功能域等进行预测和分析,能够为开展Cs NOSIP的表达及其功能研究提供理论依据。

Objective To predict the structural and functional characteristics of nitric oxide synthase interacting proteingene of Clonorchis sinensis and physical and chemical properties of its encoded protein by bioinformatics.Methods Thehomology,physicochemical property,conserved domain,signal peptide,hydrophilcity and hydrophobicity of CsNOSIP andamino acid sequence were predicted by bioinformatic analysis software such as Vector NTI suite,InterProScan,SignalP andCBS Prediction Servers.Results The open reading frame of CsNOSIP cDNA included 867 bp,coded for 288 amino acidswith theoretical molecular weight of 35 Mr and isoelectric point of 9.16.SignalP and SecretomeP analysis showed that CsNOSIP was a non-classically secreted protein.InterProScan analysis indicated the characterized NOSIP domains wererespectively located in 45~76,211~267 and 1~289 aa.Meanwhile,the predicted amino acid sequences contained sevenlinear B cell epitopes.Conclusion The bioinformatics analysis and various software may predict and analyze cDNAsequences coded by CsNOSIP and physicochemical property,structure and function domain of theoretical protein,which isavailable for providing theoretical basis of expression of CsNOSIP.