FOLDING, ASSEMBLY, AND TRANSPORT OF VIRAL GLYCOPROTEINS

当前抗病毒疫苗的改进与发展 新疫苗依赖于增加我们对病毒的了解 附着糖蛋白和融合糖蛋白。对理解的批判性洞察 通过对糖蛋白的研究，提供了糖蛋白的抗原结构。 与单抗(MAbs)相互作用。多年来，我们 研究了流感病毒血凝素(HA)糖蛋白。这 蛋白质可以作为其他具有相似功能的蛋白质的模型 (例如，HIV gp160)，而且，其本身实际上是重要的 对，因为流感仍然是发病率和死亡率的主要原因 在国内和国际上。像许多病毒糖蛋白一样，HA 是一种均低聚物，由三个相同的单体亚基组成。 在过去的一年里，我们继续调查三聚化的地点 新合成的透明质酸。我们之前发表的研究结果表明 HA三聚化只有在单体从 呃。在过去的一年里，我们使用了许多新的ER抑制剂来 高尔基复合体交通证明免疫细胞化学和 生物化学上，ERGIC(ER-的首字母缩写)中发生了三聚反应 高尔基中级车厢)。

The improvement of current antiviral vaccines and the development of novel vaccines depends on increasing our understanding of viral attachment and fusion glycoproteins. Critical insight into understanding the antigenic structure of glycoproteins is provided by studying their interaction with monoclonal antibodies (mAbs). For a number of years we have studied the influenza virus hemagglutinin (HA) glycoprotein. This protein serves as a model for other proteins with similar functions (e.g., HIV gp160), and moreover, is important practically in its own right, as influenza still is a major cause of morbidity and mortality nationally, and internationally. Like many viral glycoproteins the HA is a homo-oligomer, consisting of three identical monomeric subunits. In the past year we continued to investigate the site of trimerization of newly synthesized HA. Our previously published findings suggested that HA trimerization occurs only after monomers are exported from the ER. In the past year we have used a number of novel inhibitors of ER to Golgi complex traffic to demonstrate immunocytochemically and biochemically that trimerization occurs in the ERGIC (acronymic for ER- Golgi Intermediate Compartment).