Critical Residues Involved in the Coassembly of L1 and L2 Capsid Proteins of Human Papillomavirus 16
Jie Chen, Daning Wang, Zhiping Wang, Kunbao Wu, Shuangping Wei, Xin Chi, Ciying Qian, Yujie Xu, Lizhi Zhou, Yuqian Li, Sibo Zhang, Tingting Li, Zhibo Kong, Yingbin Wang, Qingbing Zheng, Hai Yu, Qinjian Zhao, Jun Zhang, Ningshao Xia, Shaowei Li, Ying Gu
Abstract
Over 200 types of HPV have been isolated, with several high-risk types correlated with the occurrence of cervical cancer. The HPV major capsid protein, L1, assembles into a T=7 icosahedral viral shell, and associates with the minor capsid protein, L2, which plays a critical role in the HPV life cycle. Despite the important role of the L2 protein, its structure and coassembly with L1 remain elusive. In this study, we analyzed the amino acid residues at the proposed interface between L1 and L2. Certain mutations at these sites decreased the amount of L2 protein assembled into the capsid, which, in turn, led to a decrease in viral infectivity. Knowledge about these residues and the coassembly of L1 and L2 could help to expand our understanding of HPV biology and aid in the development of countermeasures against a wide range of HPV types by targeting the L2 protein.