Burke D J, Keegstra K
J Virol. 1976 Dec;20(3):676-86. doi: 10.1128/JVI.20.3.676-686.1976.
Procedures are described for the purification of the Sindbis virus structural proteins. The amino acid and carbohydrate compositions of the purified proteins are presented for virus grown in BHK-21/13 and chicken embryo cells. Glycoprotein E1 from virus grown in BHK cells is deficient in a mannose-rich glycopeptide found on that glycoprotein when virus is grown in chicken embryo cells. The complex glactose-containing glycopeptides appear similar for virus grown in both hosts. However, when virus is grown in BHK cells, both glycoproteins are enriched in those glycopeptides containing more sialic acid. Since the two viral glycoproteins are difficult to separate cleanly during purification, it is suggested that there may be strong, but noncovalent, interactions between glycoproteins E1 and E2. It is also suggested that there may be an interaction between glycoprotein E2 and a component of the nucleocapsid.
文中描述了辛德毕斯病毒结构蛋白的纯化程序。给出了在BHK - 21/13细胞和鸡胚细胞中培养的病毒所纯化蛋白质的氨基酸和碳水化合物组成。在BHK细胞中培养的病毒的糖蛋白E1缺乏在鸡胚细胞中培养的病毒的该糖蛋白上发现的富含甘露糖的糖肽。对于在两种宿主中培养的病毒，含半乳糖的复合糖肽看起来相似。然而，当病毒在BHK细胞中培养时，两种糖蛋白都富含那些含有更多唾液酸的糖肽。由于在纯化过程中这两种病毒糖蛋白难以完全分离，表明糖蛋白E1和E2之间可能存在强烈但非共价的相互作用。还表明糖蛋白E2与核衣壳的一个成分之间可能存在相互作用。
