Cepko C L, Sharp P A
Cell. 1982 Dec;31(2 Pt 1):407-15. doi: 10.1016/0092-8674(82)90134-9.
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 three 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 molecular weight 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.
利用构象特异性单克隆抗体对腺病毒主要衣壳蛋白六邻体的组装进行了研究。六邻体壳粒是由三个相同单体组成的三聚体，折叠成高度保守且稳定的结构。壳粒与单体或变性六邻体之间缺乏共同的抗原决定簇，这表明了该结构的独特性质。三聚体的组装需要一种非病毒体蛋白，即100K蛋白的作用。病毒编码的100K蛋白与六邻体多肽形成紧密复合物。当六邻体是新生链时，这种100K-六邻体复合物可在多核糖体上形成。排阻色谱显示该复合物的分子量为800,000。该复合物仅包含前三聚体六邻体；未发现有成熟的六邻体壳粒与100K结合。对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是同时发生的。
