全蛋白组水平预测旋毛虫分泌蛋白及其功能分析  

A proteome-wide prediction and functional analysis of the secreted proteins in Trichinella spiralis

作　　者：费宏[1] 秦玉兰[1] 吴玲燕[1] 徐立新[1] 宋小凯[1] 李祥瑞[1] 严若峰[1] 

机构地区：[1]南京农业大学动物医学院,江苏南京210095

出　　处：《畜牧与兽医》2017年第4期79-84,共6页Animal Husbandry & Veterinary Medicine

基　　金：江苏省自然科学基金(BK20141365)

摘　　要：从蛋白组水平预测并分析旋毛虫分泌蛋白的特征。利用软件预测旋毛虫蛋白组范围分泌蛋白,并统计和分析其序列特征,最后利用数据库信息注释分析分泌蛋白功能。结果:预测得到414个经典途径分泌蛋白和245个非经典途径分泌蛋白,占蛋白组2.40%。MEME统计经典分泌蛋白信号肽中存在可能的3个基序。氨基酸组成分析表明,旋毛虫分泌蛋白及其信号肽主要由疏水性氨基酸组成,而信号肽剪切位点主要由亲水性氨基酸组成,信号肽剪切位点-3和-1两个位点氨基酸保守性高,可能是相关酶识别关键点。在对分泌蛋白的功能进行注释分析中发现,与核酸酶活性和蛋白酶活性相关的蛋白比例较高。研究结果为旋毛虫致病机制的深入研究提供理论基础。To predict and analyze features of secreted proteins of Trichinella spiralis on the scope of the proteomics,the procedure for predicting the secreted protein by popular bio-information software was established.After the predicting and screening of secreted proteins within the Trichinella proteomes,414 classical secreted proteins and 245 non-classical secreted proteins were found,which accounts for 2.40% of proteome.Three motifs were predicted by MEME in signal peptides of classical secretory proteins.Amino acid composition analysis revealed that T.spiralis secretory proteins and their signal peptides are mainly composed of hydrophobic amino acids,while the signal peptide cleavage sites are mainly composed of hydrophilic amino acids.The amino acids in cleavage sites-3 and-1 are highly conserved,which is possibly considered as the key points for enzyme identification.During the function annotation,a higher proportion of proteins associated with nuclease activity and protease activity were found.This study will be helpful for investigation of pathogenic factors of T.spiralis.

关 键 词：旋毛虫 蛋白组 预测 分泌蛋白 功能注释 

分 类 号：S855.99[农业科学—临床兽医学]