GLYCOSYL-PHOSPHATIDYLINOSITOL MOIETY THAT ANCHORS TRYPANOSOMA-BRUCEI VARIANT SURFACE GLYCOPROTEIN TO THE MEMBRANE
GLYCOSYL-PHOSPHATIDYLINOSITOL MOIETY THAT ANCHORS TRYPANOSOMA-BRUCEI VARIANT SURFACE GLYCOPROTEIN TO THE MEMBRANE
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DOI：
10.1126/science.3340856
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发表时间：
1988-02-12
期刊：
影响因子：
56.9
通讯作者：
RADEMACHER, TW
中科院分区：
文献类型：
--
作者：
FERGUSON, MAJ;HOMANS, SW;RADEMACHER, TW
对于真核质膜的外部糖蛋白，已经描述了两种形式的蛋白质膜锚定；即疏水性跨膜多肽和复杂的糖基磷脂酰肌醇（G-PI）部分。通过核磁共振波谱、质谱、化学修饰和外切糖苷酶消化的结合，确定了在寄生原生动物布氏锥虫的单一变异表面糖蛋白 (VSG) 上发现的主要 G-PI 锚物种的化学结构。发现 G-PI 锚在单糖序列方面是异质的，并且存在一些新的糖苷键。该结果与 G-PI 锚的生物合成机制相关。
Two forms of protein-membrane anchor have been described for the externally disposed glycoproteins of eukaryotic plasma membranes; namely, the hydrophobic transmembrane polypeptide and the complex glycosylphosphatidylinositol (G-PI) moiety. The chemical structures of the major species of G-PI anchors found on a single variant surface glycoprotein (VSG) of the parasitic protozoan Trypanosoma brucei were determined by a combination of nuclear magnetic resonance spectroscopy, mass spectrometry, chemical modification, and exoglycosidase digestions. The G-PI anchor was found to be heterogeneous with respect to monosaccharide sequence, and several novel glycosidic linkages were present. The results are pertinent to the mechanism of the biosynthesis of G-PI anchors.