Structure of the glycosylphosphatidylinositol anchor of the Trypanosoma brucei transferrin receptor
Structure of the glycosylphosphatidylinositol anchor of the Trypanosoma brucei transferrin receptor
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DOI：
10.1016/j.molbiopara.2006.11.001
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发表时间：
2007-02-01
影响因子：
1.5
通讯作者：
Ferguson, Michael A. J.
中科院分区：
文献类型：
--
作者：
Mehlert, Angela;Ferguson, Michael A. J.
采用高灵敏度非印迹法测定了锥虫转铁蛋白受体ESAG（表达位点相关基因）6组分的糖基磷脂酰肌醇（GPI）锚点的结构，并与其他锥虫糖蛋白的结构进行了比较。结果表明，ESAG GPI锚点携带己糖（可能是半乳糖）侧链，并且修饰程度略大于变异的表面糖蛋白（VSG） 221， VSG变体具有迄今为止表征的半乳糖化程度最高的GPI锚点。此外，ESAG 6 GPI糖型模式似乎独立于常驻VSG。这些数据加强了一种假设，即新合成的gpi锚定蛋白的c端结构域的三维结构控制了血流形成t内质网和高尔基体中组成性表达的gpi修饰α-和β-半乳糖转移酶的进入。brucei。ESAG6的GPI锚定将基于含有糖脂A前体的sn-1,2-二肉豆醇- pi重塑的脂肪酸。
The structure of the glycosylphosphatidylinositol (GPI) anchor of the ESAG (expression site associated gene) 6 component of the trypanosome transferrin receptor was determined using the high sensitivity off-blot methodology and was compared to those found on other trypanosome glycoproteins. Results showed that the ESAG GPI anchor carries hexose (presumably galactose) side chains and that the extent of modification is slightly greater than that variant surface glycoproteins (VSG) 221, the VSG variant with the most highly galactosylated GPI anchor thus far characterized. Furthermore, it appears that the ESAG 6 GPI glycoform pattern is independent of that of the resident VSG. These data strengthen the hypothesis that the three-dimensional structure of the C-terminal domain of a newly synthesized GPI-anchored protein controls the access of constitutively expressed GPI-modifying α- and β-galactosyltransferases in the endoplasmic reticulum and golgi apparatus of bloodstream formT. brucei. The GPI anchor of ESAG6 would be based on the fatty acid remodelledsn-1,2-dimyristoyl-PI containing glycolipid A precursor.