STRUCTURE OF A PLASMODIUM-CHABAUDI ACIDIC PHOSPHOPROTEIN THAT IS ASSOCIATED WITH THE HOST ERYTHROCYTE-MEMBRANE
STRUCTURE OF A PLASMODIUM-CHABAUDI ACIDIC PHOSPHOPROTEIN THAT IS ASSOCIATED WITH THE HOST ERYTHROCYTE-MEMBRANE
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DOI：
10.1016/0166-6851(92)90154-c
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发表时间：
1992-11-01
影响因子：
1.5
通讯作者：
HAMERS, R
中科院分区：
文献类型：
--
作者：
DELEERSNIJDER, W;PRASOMSITTI, P;HAMERS, R
我们的特点是分子克隆和测序的夏氏疟原虫抗原，是与整个红细胞内循环感染的红细胞膜。该蛋白质（PcEMA 1）具有50 kDa的预测大小，并包含一个主要的串联重复阵列的16个八肽，构成几乎30%的蛋白质。在其氨基末端，PcEMA 1具有一串分泌蛋白的特征性疏水残基，但不包含疏水跨膜区段。抗原似乎位于红细胞膜的胞质表面。PcEMA 1的预测pI为4.4，是一种潜在的磷蛋白。
We have characterized by molecular cloning and sequencing a Plasmodium chabaudi antigen that is associated with the membrane of the infected erythrocyte throughout the entire intraerythrocytic cycle. The protein (PcEMA1) has a predicted size of 50 kDa and contains a major tandem repeat array of 16 octapeptides that constitutes almost 30% of the protein. At its amino-terminus, PcEMA1 has a string of hydrophobic residues characteristic of a secreted protein, but does not contain a hydrophobic membrane-spanning segment. The antigen appears to reside on the cytoplasmic face of the erythrocytic membrane. PcEMA1 has a predicted pI of 4.4 and is a potential phosphoprotein.