Study of proteins associated with the Eimeria tenella refractile body by a proteomic approach

Study of proteins associated with the Eimeria tenella refractile body by a proteomic approach
复制标题

DOI:
10.1016/j.ijpara.2006.06.018
复制
发表时间:
2006-11-01
影响因子:
4
通讯作者:
Labbe, Marie
Labbe, Marie
中科院分区:
医学2区
文献类型:
--
作者:
de Venevelles, Patrick;Chich, Jean Francois;Labbe, Marie

文献摘要

被引文献

相似文献

屈光体(Rb)是艾美耳球虫寄生虫特有的结构,其功能尚不清楚。为研究柔嫩艾美耳球虫子孢子Rb的蛋白质组学特性,采用可逆固定-离心法从柔嫩艾美耳球虫子孢子中分离纯化Rb。用双向电泳法对Rb蛋白进行分离。分别使用3-10和4-7范围内的梯度在RB二维凝胶上检测到大约76个和89个斑点。Rb蛋白主要位于pH 5和7之间。然后将Rb凝胶与先前建立的整个子孢子蛋白质组图谱进行比较。用质谱仪鉴定出现在新斑点上的蛋白质。Rb有30种蛋白质异构体。在已知的Rb蛋白如Eimepsin和SOT的基础上,新的Rb蛋白被定义为卤酸脱卤酶、水解酶、枯草杆菌酶、内酯脱氢酶或泛素家族蛋白。Rb蛋白质组分析证实了这种结构是入侵所必需蛋白质的储存库的假设,但也表明Rb具有能量和代谢功能。(C)2006澳大利亚寄生虫学协会。爱思唯尔有限公司出版。版权所有。
Refractile bodies (RB), whose function is still unknown, are specific structures of Eimeriidae parasites. In order to study their proteome, RB were purified from Eimeria tenella sporozoites by a new procedure using a reversible fixation followed by centrifugation. RB proteins were resolved by two-dimensional electrophoresis. Around 76 and 89 spots were detected on RB two-dimensional gels using gradients in the 3-10 and 4-7 range, respectively. RB proteins were located mainly between pH 5 and 7. RB gels were then compared with previously established maps of the entire sporozoite proteome. Proteins appearing in new spots were identified by mass spectrometry. Thirty protein isoforms were located in RB. Added to the already known RB proteins such as Eimepsin and SOT, the new RB proteins were defined as haloacid dehalogenase, hydrolase, subtilase, lactacte dehydrogenase or ubiquitin family proteins. The RB proteome analysis confirmed the hypothesis that this structure is a reservoir for proteins necessary to invasion but also suggests that RB have energetic and metabolic functions. (c) 2006 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved.