Characterization of a modified red cell membrane protein expressed on erythrocytes infected with the human malaria parasite Plasmodium falciparum: possible role as a cytoadherent mediating protein.
Characterization of a modified red cell membrane protein expressed on erythrocytes infected with the human malaria parasite Plasmodium falciparum: possible role as a cytoadherent mediating protein.
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感染人类疟原虫恶性疟原虫的红细胞上表达的修饰红细胞膜蛋白的表征：作为细胞粘附介导蛋白的可能作用。
DOI：
10.1083/jcb.108.1.23
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
Sherman,IW
中科院分区：
文献类型：
--
作者：
Winograd,E;Sherman,IW
感染人疟疾恶性疟原虫的特征是寄生的红细胞滞留在组织毛细血管和小静脉中。含有滋养体和滋养体的红细胞通过存在于受感染细胞表面上的结构上可识别的赘生物附着于内衬这些血管的内皮细胞。这种赘生物，通常被称为旋钮，可以通过扫描或透射电子显微镜观察到。红细胞粘附于内皮细胞的生化机制尚不清楚。为了鉴定感染细胞表面的细胞粘附分子，我们制备了抗FCR-3型恶性疟原虫株感染的带有结节的红细胞的单克隆抗体。这些单克隆抗体之一，被设计为4A 3，是一种IgM，其与携带多节系成熟寄生虫的未固定红细胞表面反应（通过免疫荧光）;它不与无节系或未感染的红细胞反应。通过免疫电子显微镜，单克隆抗体4A 3被定位于球区域。在体外细胞粘附试验中，单克隆抗体部分阻断了结轴承细胞（FCR-3株）与福尔马林固定的无黑色素黑色素瘤细胞的结合。该单克隆抗体用于免疫沉淀来自先前表面碘化的多节红细胞提取物的蛋白质。通过二维肽图技术，单克隆抗体识别的抗原被发现在结构上与人红细胞阴离子转运蛋白带3蛋白相关。
Infections with the human malaria Plasmodium falciparum are characterized by the retention of parasitized erythrocytes in tissue capillaries and venules. Erythrocytes containing trophozoites and schizonts attach to the endothelial cells that line these vessels by means of structurally identifiable excrescences present on the surface of the infected cell. Such excrescences, commonly called knobs, are visible by means of scanning or transmission electron microscopy. The biochemical mechanisms responsible for erythrocyte adherence to the endothelial cell are still undefined. In an attempt to identify the cytoadhesive molecule on the surface of the infected cell, we have prepared monoclonal antibodies to knob-bearing erythrocytes infected with the FCR-3 strain of P. falciparum. One of these monoclonal antibodies, designed 4A3, is an IgM that reacts (by means of immunofluorescence) with the surface of unfixed erythrocytes bearing mature parasites of the knobby line; it does not react with knobless lines or uninfected erythrocytes. By immunoelectron microscopy the monoclonal antibody 4A3 was localized to the knob region. In an in vitro cytoadherence assay, the monoclonal antibody partially blocked the binding of knob-bearing cells (FCR-3 strain) to formalin-fixed amelanotic melanoma cells. The monoclonal antibody was used to immunoprecipitate a protein from extracts of knobby erythrocytes that had been previously surface iodinated. By a two-dimensional peptide mapping technique, the antigen recognized by the monoclonal antibody was found to be structurally related to band 3 protein, the human erythrocyte anion transporter.