本文選題：旋毛蟲 + 蛋白組　； 參考：《畜牧與獸醫(yī)》2017年04期

【摘要】：從蛋白組水平預(yù)測并分析旋毛蟲分泌蛋白的特征。利用軟件預(yù)測旋毛蟲蛋白組范圍分泌蛋白,并統(tǒng)計和分析其序列特征,最后利用數(shù)據(jù)庫信息注釋分析分泌蛋白功能。結(jié)果:預(yù)測得到414個經(jīng)典途徑分泌蛋白和245個非經(jīng)典途徑分泌蛋白,占蛋白組2.40%。MEME統(tǒng)計經(jīng)典分泌蛋白信號肽中存在可能的3個基序。氨基酸組成分析表明,旋毛蟲分泌蛋白及其信號肽主要由疏水性氨基酸組成,而信號肽剪切位點主要由親水性氨基酸組成,信號肽剪切位點-3和-1兩個位點氨基酸保守性高,可能是相關(guān)酶識別關(guān)鍵點。在對分泌蛋白的功能進行注釋分析中發(fā)現(xiàn),與核酸酶活性和蛋白酶活性相關(guān)的蛋白比例較高。研究結(jié)果為旋毛蟲致病機制的深入研究提供理論基礎(chǔ)。
[Abstract]:The characteristics of Trichinella spiralis secretory protein were predicted and analyzed from the proteome level.The software was used to predict the secretory proteins of Trichinella spiralis, and the sequence characteristics of them were analyzed. Finally, the function of secreting proteins was analyzed by annotating the database information.Results: a total of 414 classical pathway secretory proteins and 245 non-classical pathway secreted proteins were predicted, accounting for three possible motifs in the 2.40%.MEME of the protein group.Amino acid composition analysis showed that the secreted protein and its signal peptide of Trichinella spiralis were mainly composed of hydrophobic amino acids, while the signal peptide shearing sites were mainly composed of hydrophilic amino acids, and the amino acids of signal peptide shearing sites-3 and -1 were highly conserved.It may be the key point of enzyme recognition.In the analysis of the function of secretory protein, it was found that the proportion of protein related to nuclease activity and protease activity was high.The results provide a theoretical basis for the further study of the pathogenic mechanism of Trichinella spiralis.
【作者單位】： 南京農(nóng)業(yè)大學(xué)動物醫(yī)學(xué)院;
【基金】：江蘇省自然科學(xué)基金(BK20141365)
【分類號】：S852.7

【參考文獻】

相關(guān)期刊論文 前4條

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本文編號：1766337