Schwarz R T, Schmidt M F, Anwer U, Klenk H D
J Virol. 1977 Aug;23(2):217-26. doi: 10.1128/JVI.23.2.217-226.1977.
The carbohydrate moiety of the influenza glycoproteins NA, HA(1), and HA(2) were analyzed by labeling with radioactive sugars. Analysis of glycopeptides obtained after digestion with Pronase indicated that there are at least two different types of carbohydrate side chains. The side chain of type I is composed of glucosamine, mannose, galactose, and fucose. It is found on NA, HA(1), and HA(2). The side chain of type II contains a high amount of mannose and is found only on NA and HA(2). The molecular weights of the corresponding glycopeptides obtained from virus grown in chicken embryo cells are 2,600 for type I and 2,000 for type II. The glycoproteins of virus grown in MDBK cells have a higher molecular weight than those of virus grown in chicken embryo cells, and there is a corresponding difference in the molecular weights of the glycopeptides. Under conditions of partial inhibition of glycosylation, virus particles were isolated that contained hemagglutinin with reduced carbohydrate content. Glycopeptide analysis indicated that this reduction is due to the lack of whole carbohydrate side chains and not to the incorporation of incomplete ones. This observation suggests that glycosylation of the viral glycoproteins involves en bloc transfer of the core sugars to the polypeptide chains.
通过用放射性糖标记对流感病毒糖蛋白神经氨酸酶(NA)、血凝素1(HA(1))和血凝素2(HA(2))的碳水化合物部分进行了分析。用链霉蛋白酶消化后得到的糖肽分析表明,至少存在两种不同类型的碳水化合物侧链。I型侧链由氨基葡萄糖、甘露糖、半乳糖和岩藻糖组成。它存在于NA、HA(1)和HA(2)上。II型侧链含有大量甘露糖,仅存在于NA和HA(2)上。从鸡胚细胞中生长的病毒获得的相应糖肽的分子量,I型为2600,II型为2000。在MDBK细胞中生长的病毒的糖蛋白分子量比在鸡胚细胞中生长的病毒的糖蛋白分子量更高,并且糖肽的分子量也存在相应差异。在部分糖基化抑制的条件下,分离出了碳水化合物含量降低的含有血凝素的病毒颗粒。糖肽分析表明,这种降低是由于缺乏完整的碳水化合物侧链,而不是由于掺入了不完整的侧链。这一观察结果表明,病毒糖蛋白的糖基化涉及核心糖向多肽链的整体转移。