Application of two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for proteomic analysis of the sexually transmitted parasite Trichomonas vaginalis
Application of two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for proteomic analysis of the sexually transmitted parasite Trichomonas vaginalis
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DOI：
10.1002/jms.1286
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发表时间：
2007-11-01
影响因子：
2.3
通讯作者：
Domont, Gilberto Barbosa
中科院分区：
文献类型：
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作者：
De Jesus, Jose Batista;Cuervo, Patricia;Domont, Gilberto Barbosa
阴道毛滴虫是一种性传播的原生动物寄生虫，感染人类泌尿生殖道，引起滴虫病，这是一种世界性疾病。本文利用一株新鲜临床分离的阴道绦虫对其蛋白表达进行了研究。采用二维凝胶电泳（2-DE）和MALDI-TOF/TOF质谱（MS）建立pH范围为4-7的可溶性蛋白参考图谱。通过肽质量指纹图谱和串联质谱技术，鉴定出了116个高丰度和低丰度表达的功能类蛋白，这些蛋白对应67种不同的蛋白，表明阴道T.翻译后修饰是阴道T.翻译后修饰的普遍现象。根据生物过程将鉴定出的蛋白质分为16类。在检测到的蛋白质中，我们确定了参与细胞质和氢基因体代谢途径的主要酶，以及可能用于新药设计的蛋白质靶点。此外，该分析允许验证先前的基因预测，确认15种假设蛋白质的表达。最后，本文的研究结果代表了阴道绦虫的第一个参考蛋白质组图，并为描述该寄生虫的综合蛋白质组图迈出了第一步。版权所有(C) 2007约翰威利父子有限公司
Trichomonas vaginalis is a sexually transmitted protozoan parasite that infects the human urogenital tract causing trichomoniasis, a worldwide disease. In this work, a fresh clinical isolate of T. vaginalis was used for study of the protein expression in this species. Two-dimensional gel electrophoresis (2-DE) and MALDI-TOF/TOF mass spectrometry (MS) were employed to create a reference map of soluble proteins in the pH range 4-7. A set of 116 proteins belonging to functional classes expressed in high and low abundance was identified by peptide mass fingerprinting and tandem MS. These identifications corresponded to 67 different proteins, suggesting that post-translational modifications are common phenomena in T. vaginalis. Identified proteins were classified into 16 groups according to biological processes. Among detected proteins we identified the major enzymes involved in both cytosolic and hydrogenosomal metabolic pathways, as well as putative protein targets for new drug design. In addition, this analysis allows validation of previous gene predictions confirming the expression of 15 hypothetical proteins. Finally, the findings here reported represent the first reference proteome map of T. vaginalis and the first steps towards the description of a comprehensive proteome map of this parasite. Copyright (C) 2007 John Wiley & Sons, Ltd.