OLIGOMERIZATION OF THE HUMAN CYTOMEGALOVIRUS MAJOR ENVELOPE GLYCOPROTEIN COMPLEX GB (GP55-116)
OLIGOMERIZATION OF THE HUMAN CYTOMEGALOVIRUS MAJOR ENVELOPE GLYCOPROTEIN COMPLEX GB (GP55-116)
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DOI：
10.1128/jvi.66.11.6747-6754.1992
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发表时间：
1992-11-01
影响因子：
5.4
通讯作者：
VUGLER, LG
中科院分区：
文献类型：
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作者：
BRITT, WJ;VUGLER, LG
人巨细胞病毒的二硫化物连接糖蛋白B （gB; gp55-116）复合物是病毒粒子包膜中最丰富和最具免疫原性的成分。我们利用一系列小鼠单克隆抗体研究了该分子的寡聚化和转运。我们的结果表明，该分子在合成后不久就发生了寡聚化，最大形成的半衰期约为25分钟。低聚形式估计质量为340,000 Da，可能由gp55-116复合物的同型二聚体组成。利用构象特异性单克隆抗体，证实了该分子的后寡聚折叠。该事件表现出异常延长的半最大时间约为160分钟。寡聚化和折叠都发生在内质网。低聚和折叠发生在没有碳水化合物修饰的情况下，尽管效率可能较低。最后，寡聚和折叠形式被证明被运输到感染细胞的表面
The disulfide-linked glycoprotein B (gB; gp55-116) complex of human cytomegalovirus represents the most abundant and immunogenic component of the virion envelope. We have studied the oligomerization and transport of this molecule, using a series of murine monoclonal antibodies. Our results indicated that oligomerization of this molecule occurred shortly after its synthesis, with a half-time of maximal formation of approximately 25 min. The oligomeric form had an estimated mass of 340,000 Da and likely consisted of a homodimer of the gp55-116 complex. By using a conformation-specific monoclonal antibody, postoligomerization folding of this molecule was demonstrated. This event exhibited an unusually prolonged half-maximal time of approximately 160 min. Both oligomerization and folding occurred in the endoplasmic reticulum. Oligomerization and folding occurred in the absence of carbohydrate modifications, although likely at lower efficiency. Finally, the oligomeric and folded forms were shown to be transported to the surface of infected cells