Calnexin associates with the precursors of glycoproteins B, C, and D of herpes simplex virus type 1.

Calnexin associates with the precursors of glycoproteins B, C, and D of herpes simplex virus type 1.
复制标题

钙连接蛋白与 1 型单纯疱疹病毒糖蛋白 B、C 和 D 的前体相关。

DOI:
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发表时间:
1996
期刊:
影响因子:
3.7
通讯作者:
Y. Nishiyama
Y. Nishiyama
中科院分区:
医学3区
文献类型:
--
作者:
Y. Yamashita;M. Yamada;T. Daikoku;H. Yamada;A. Tadauchi;T. Tsurumi;Y. Nishiyama

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通过结合免疫沉淀的脉冲追踪方法,我们发现新合成的单纯疱疹病毒1型(HSV-1)糖蛋白B(gB)、糖蛋白C(gC)和糖蛋白D(gD)的前体与钙连接蛋白(内质网中的膜结合伴侣)相关。前体之间的缔合和解离动力学是相当不同的。对于HSV-1的gC和gD的前体,在合成后立即观察到最大缔合,并且它们迅速解离,其中gC的半衰期为25 min,gD的半衰期为30 min。相比之下,gB的前体显示出与钙连接蛋白的长期关联。合成后30分钟观察到它们的最大结合,此后,它们缓慢解离,半衰期为70分钟。结果表明,虽然具有快速加工速率的糖蛋白,如HSV-1的gC和gD,与钙连接蛋白快速结合,并且它们的结合非常短,但那些需要很长时间才能加工成成熟形式的糖蛋白,如HSV-1的gB,与钙连接蛋白具有延长的结合动力学。完全抑制这些糖蛋白前体钙连接蛋白的结合衣霉素或栗精胺表明部分修剪的N-连接寡糖的重要性,他们的协会。
By a pulse-chase approach combined with immunoprecipitation, we showed that the newly synthesized precursors of glycoprotein B (gB), glycoprotein C (gC), and glycoprotein D (gD) of herpes simplex virus type 1 (HSV-1) were associated with calnexin, a membrane-bound chaperone in the endoplasmic reticulum. Kinetics of association and dissociation was quite different among the precursors. For the precursors of gC and gD of HSV-1, the maximal association was observed immediately after the synthesis and they dissociated rapidly with half-times of 25 min for gC and 30 min for gD, respectively. In contrast, the precursor of gB showed prolonged association with calnexin. Their maximum association was observed 30 min after the synthesis, and thereafter, they dissociated slowly with a half-time of 70 min. The results suggest that, while glycoproteins that have a rapid processing rate, such as gC and gD of HSV-1, rapidly associate with calnexin and their association is quite short, those that take much time to be processed to a mature form, such as gB of HSV-1, have prolonged association kinetics with calnexin. Complete inhibition of the binding of these glycoprotein precursors to calnexin by tunicamycin or castanospermine indicates the importance of partially trimmed N-linked oligosaccharides for their association.