Hakimi J, Atkinson P H
Biochemistry. 1982 Apr 27;21(9):2140-5. doi: 10.1021/bi00538a024.
Oligosaccharides of purified intracellular Sindbis virus glycoproteins have been examined by high-resolution Bio-Gel chromatography. The array of glycopeptides from cellular E1 and E2 appeared similar to the glycopeptides (S1, S2, S3, and S4) found in mature virus glycoproteins described previously [Hakimi, J., & Atkinson, P. H. (1980) Biochemistry 19, 5619]. However, compared to its viral counterpart, intracellular E1 glycoprotein also contained larger sized mannosyl oligosaccharides. B and PE2 proteins were found to contain an array of primarily large mannosyl oligosaccharides (8-10 hexose units). No sialyl glycopeptides were found on these proteins regardless of labeling time. By contrast, the products of PE2 cleavage (E2 and E3) contained sialyl glycopeptides similar to those found in mature virus (S1, S2, and S3). E2 also contained smaller mannosyl oligosaccharides (8-5 hexose units) similar to its viral counterpart. Current evidence shows that sialyl and galactosyl transferases are in or near the Golgi region. Thus we conclude that cleavage of PE2 with a Man8 oligosaccharide structure occurs in the Golgi region and not in the plasma membrane as suggested by others.
通过高分辨率生物凝胶色谱法对纯化的细胞内辛德毕斯病毒糖蛋白的寡糖进行了检测。来自细胞E1和E2的糖肽阵列与先前描述的成熟病毒糖蛋白中发现的糖肽（S1、S2、S3和S4）相似[哈基米，J.，&阿特金森，P. H.（1980年）《生物化学》19，5619]。然而，与病毒对应物相比，细胞内E1糖蛋白还含有更大尺寸的甘露糖基寡糖。发现B和PE2蛋白主要含有一系列大的甘露糖基寡糖（8 - 10个己糖单位）。无论标记时间如何，在这些蛋白上均未发现唾液酸糖肽。相比之下，PE2裂解产物（E2和E3）含有与成熟病毒中发现的类似的唾液酸糖肽（S1、S2和S3）。E2还含有与其病毒对应物相似的较小的甘露糖基寡糖（8 - 5个己糖单位）。目前的证据表明，唾液酸转移酶和半乳糖基转移酶位于高尔基体区域或其附近。因此我们得出结论，具有Man8寡糖结构的PE2裂解发生在高尔基体区域，而不是如其他人所认为的在质膜中。
