Liu J F, Lu Y Q, Roth E F, Nagel R L, Blumenfeld O O
Department of Biochemistry, Hunan Medical University, Changsha.
Chin Med J (Engl). 1993 Apr;106(4):307-12.
The extent of participation and changes of glycophorins (GPs) and membrane proteins in the merozite-human erythrocyte interaction during the invasion of Plasmodium falciparum (Pf) were studied by immunoblotting techniques. Polyclonal antisera to alpha GP and to its C-terminal fragment (residues 82-131) as well as M and N specific monoclonal antibodies (MoAbs) were used. We examined the GPs in the parasite-free saponin lysates, saponin pellets and the culture supernatants of the infected erythrocytes in comparison with the mock cultured normal RBC. Excepting the usual GP patterns, a GP with molecular weight of 77.5 K (band 1') existed in the parasitized erythrocytes and their saponin pellets and several GP bands ranging from 28K to 54K were present in saponin pellets when probed with anti-GP and anti-peptide C sera. This reflected the disintegration of erythrocyte membrane alpha GP through the invasion of Pf. The alpha 2 GP in the saponin pellets of the parasitized MM erythrocytes surprisingly cross-reacted with the N MoAb, implying that it may have come from the intermingling of the host alpha GP in MM erythrocytes with the parasite alpha GP reacting to N MoAb. The saponin pellets of parasitized erythrocytes preserved a considerable amount of ankyrin, band 3, protein 4.1 and 4.2, while the GP bands were densely mixed with the parasite proteins and the disintegrated products of membrane proteins. Four erythrocyte-binding antigens (EBA) of 143 K, 135 K, 115 K and 107 K recognized by malaria hyperimmune serum were detected in the culture supernatants of Pf, some of them appeared in the infected erythrocytes, their saponin lysates and pellets.
通过免疫印迹技术研究了恶性疟原虫（Pf）入侵期间糖蛋白（GPs）和膜蛋白在裂殖子 - 人红细胞相互作用中的参与程度和变化。使用了针对α GP及其C末端片段（第82 - 131位氨基酸残基）的多克隆抗血清以及M和N特异性单克隆抗体（MoAbs）。与模拟培养的正常红细胞相比，我们检测了无寄生虫的皂素裂解物、皂素沉淀以及感染红细胞的培养上清液中的GPs。除了常见的GP模式外，在用抗GP和抗肽C血清检测时，寄生红细胞及其皂素沉淀中存在分子量为77.5 K的GP（条带1'），皂素沉淀中还存在几条分子量在28K至54K之间的GP条带。这反映了Pf入侵导致红细胞膜α GP的分解。寄生的MM红细胞皂素沉淀中的α2 GP与N MoAb意外地发生交叉反应，这意味着它可能来自MM红细胞中宿主α GP与对N MoAb起反应的寄生虫α GP的混合。寄生红细胞的皂素沉淀保留了相当数量的锚蛋白、带3蛋白、蛋白4.1和4.2，而GP条带与寄生虫蛋白和膜蛋白的分解产物紧密混合。在Pf的培养上清液中检测到了疟疾超免疫血清识别的四种红细胞结合抗原（EBA），分子量分别为143 K、135 K、115 K和107 K，其中一些出现在感染的红细胞、其皂素裂解物和沉淀中。
