CHARACTERIZATION OF MICRONEME PROTEINS OF TOXOPLASMA-GONDII
CHARACTERIZATION OF MICRONEME PROTEINS OF TOXOPLASMA-GONDII
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DOI：
10.1016/0166-6851(91)90182-6
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发表时间：
1991-08-01
影响因子：
1.5
通讯作者：
DUBREMETZ, JF
中科院分区：
文献类型：
--
作者：
ACHBAROU, A;MERCEREAUPUIJALON, O;DUBREMETZ, JF
用3种单克隆抗体和重组蛋白特异性抗血清对弓形虫的3种微线体蛋白进行了鉴定。在所有情况下，顶端标记的速殖子和缓殖子观察到间接免疫荧光法。免疫胶体金定位于缓殖子或速殖子的切片上，显示微线体的特异性标记。使用二维凝胶电泳和蛋白质免疫印迹表征以下蛋白质：Mic 1（60 kDa，Pi 6.5）、Mic 2（120 kDa，Pi 5）和Mic 3（90 kDa，Pi 6.75）。90-kDa蛋白（Mic 3）是由二硫键连接的两个38-kDa多肽（Pi分别为6.7和6.75）的异源二聚体。代谢标记和免疫沉淀试验表明，至少有一个38 kDa的多肽是从40 kDa的前体加工。在120-和60-kDa多肽的生物合成过程中没有观察到加工。
Three microneme proteins of Toxoplasma gondii have been characterized using 3 monoclonal antibodies and a recombinant protein specific antiserum. In all cases, apical labeling of tachyzoites and bradyzoites was observed by indirect immunofluorescence assay. Immunogold localization on ultrathin sections of bradyzoites or tachyzoites showed a specific labeling of micronemes. The following proteins were characterized using 2-dimensional gel electrophoresis and Western immunoblotting: Mic 1 (60 kDa, Pi 6.5), Mic 2 (120 kDa, Pi 5) and Mic 3 (90 kDa, Pi 6.75). The 90-kDa protein (Mic 3) is a heterodimer of two 38-kDa polypeptides (Pi 6.7 and 6.75 respectively) linked by disulfide bridges. Metabolic labeling and immunoprecipitation assays showed that at least one of the 38-kDa polypeptides was processed from a 40-kDa precursor. No processing was observed during the biosynthesis of the 120- and 60-kDa polypeptides.