Zhou Z H, He J, Jakana J, Tatman J D, Rixon F J, Chiu W
Texas Center for Advanced Molecular Computation, University of Houston, Texas 77204-3476, USA.
Nat Struct Biol. 1995 Nov;2(11):1026-30. doi: 10.1038/nsb1195-1026.
The 1250 A diameter herpes simplex virus-1 (HSV-1) capsid shell consists of four major structural proteins, of which VP26 (approximately 12,000 M(r)) is the smallest. Using 400 kV electron cryomicroscopy and computer reconstruction, we have determined the three-dimensional structures of the wild-type capsid and a recombinant baculovirus-generated HSV-1 capsid which lacks VP26. Their difference map demonstrates the presence of VP26 hexamers attached to all the hexons in the wild-type capsid, and reveals that the VP26 molecule consists of a large and a small domain. Although both hexons and pentons are predominantly composed of VP5, VP26 is not present on the penton. Based on the interactions involving VP26 and the hexon subunits, we propose a mechanism for VP26 assembly which would account for its distribution. Possible roles of VP26 in capsid stability and DNA packaging are discussed.
直径为1250埃的单纯疱疹病毒1型（HSV-1）衣壳由四种主要结构蛋白组成，其中VP26（约12,000 M(r)）是最小的。利用400 kV电子冷冻显微镜和计算机重建技术，我们确定了野生型衣壳和一种缺乏VP26的重组杆状病毒产生的HSV-1衣壳的三维结构。它们的差异图显示野生型衣壳中所有六邻体上都附着有VP26六聚体，并揭示VP26分子由一个大结构域和一个小结构域组成。虽然六邻体和五邻体主要由VP5组成，但五邻体上不存在VP26。基于涉及VP26和六邻体亚基的相互作用，我们提出了一种VP26组装机制，该机制可以解释其分布情况。还讨论了VP26在衣壳稳定性和DNA包装中的可能作用。
