ASSEMBLY OF ADENOVIRUS MAJOR CAPSID PROTEIN IS MEDIATED BY A NONVIRION PROTEIN
ASSEMBLY OF ADENOVIRUS MAJOR CAPSID PROTEIN IS MEDIATED BY A NONVIRION PROTEIN
复制标题
DOI：
10.1016/0092-8674(82)90134-9
复制
发表时间：
1982-01-01
期刊：
影响因子：
64.5
通讯作者：
SHARP, PA
中科院分区：
文献类型：
--
作者：
CEPKO, CL;SHARP, PA
利用构象特异性单克隆抗体研究了腺病毒主要衣壳蛋白六邻体的组装。六邻体壳粒是3个相同单体的三聚体，折叠成高度保守和稳定的结构。这种结构的独特性质是由壳粒和单体或变性六邻体之间缺乏共同的抗原决定簇指示的。三聚体的组装需要非病毒体蛋白100 K蛋白的作用。病毒编码的100 K蛋白与六邻体多肽形成紧密复合物。这种100 K-六邻体复合物可以在多聚核糖体上形成，而六邻体是新生链。排阻色谱显示该复合物的分子量为800，000。该复合物只含有前三聚体六邻体，没有发现成熟的六邻体壳粒与100 K结合。六邻体三聚化和六邻体-100K结合的动力学分析表明，三聚化和六邻体从复合物中的释放伴随发生。
The assembly of hexon, the major capsid protein of adenovirus, was investigated with the use of conformation-specific monoclonal antibodies. The hexon capsomere is a trimer of 3 identical monomers folded into a highly conserved and stable structure. The unique nature of this structure is indicated by the lack of common antigenic determinants between the capsomere and either monomeric or denatured hexon. The assembly of the trimer requires the action of a nonvirion protein, the 100K protein. The virus-encoded 100K protein forms a tight complex with hexon polypeptides. This 100K-hexon complex can form on the polyribosomes while hexon is a nascent chain. Exclusion chromatography revealed that the complex has a MW of 800,000. The complex contains only pretrimer hexon; no mature hexon capsomeres can be found bound to 100K. Kinetic analysis of hexon trimerization and hexon-100K binding indicated that trimerization and the release of hexon from the complex occur concomitantly.