Wathen M W, Aeed P A, Elhammer A P
Upjohn Company, Kalamazoo, Michigan 49001.
Biochemistry. 1991 Mar 19;30(11):2863-8. doi: 10.1021/bi00225a019.
The oligosaccharide structures added to a chimeric protein (FG) composed of the extracellular domains of respiratory syncytial virus F and G proteins, expressed in the insect cell line Sf9, were investigated. Cells were labeled in vivo with [3H]glucosamine and infected with a recombinant baculovirus containing the FG gene. The secreted chimeric protein was isolated by immunoprecipitation and subjected to oligosaccharide analysis. The FG protein contains two types of O-linked oligosaccharides: GalNAc and Gal beta 1-3GalNAc constituting 17 and 66% of the total number of structures, respectively. Only one type of N-linked oligosaccharide, constituting the remaining 17% of the structures on FG, was detected: a trimannosyl core structure with a fucose residue linked alpha 1-6 to the asparagine-linked N-acetylglucosamine.
对在昆虫细胞系Sf9中表达的、由呼吸道合胞病毒F和G蛋白的胞外结构域组成的嵌合蛋白（FG）所添加的寡糖结构进行了研究。用[3H]葡糖胺在体内标记细胞，并用含有FG基因的重组杆状病毒进行感染。通过免疫沉淀分离分泌的嵌合蛋白，并进行寡糖分析。FG蛋白含有两种类型的O-连接寡糖：GalNAc和Galβ1-3GalNAc，分别占结构总数的17%和66%。仅检测到一种类型的N-连接寡糖，占FG上结构的其余17%：一种三甘露糖核心结构，其岩藻糖残基以α1-6连接至天冬酰胺连接的N-乙酰葡糖胺。
