Insights into varicella-zoster virus assembly from the B- and C-capsid at near-atomic resolution structures
Lei Cao, Nan Wang, Zhe Lv, Wenyuan Chen, Zhonghao Chen, Lifei Song, Xueyan Sha, Guiqiang Wang, Yaling Hu, Xiaojun Lian, Guoliang Cui, Jinyan Fan, Yaru Quan, Hongrong Liu, Hai Hou, Xiangxi Wang
Abstract
Varicella-zoster is a highly communicable virus that can be transmitted through the airborne route. About one quarter of people are infected with this virus. Previous studies have described the structure of A-capsid and a blurred reconstruction of the C-capsid with icosahedral symmetry. In this study, we have determined the more precise detailed structures of the varicella-zoster virus (VZV) B- and C-capsid in icosahedral symmetry using a combination of block-based reconstruction and symmetry relaxation strategies. In addition, we are reporting structural details of the portal vertex reconstructions in five-fold symmetry and portal reconstructions in twelve-fold symmetry. The structures unveil the basis for the high thermal stability of the VZV capsid. The conformational flexibility of structural elements of the capsid plays a role in the assembly of the capsid and drives processes critical for the viral life cycle. The results of the study open up new avenues for the development of drugs against a highly prevalent and contagious pathogen.