5JB1

Pseudo-atomic structure of Human Papillomavirus Type 59 L1 Virus-like Particle

Summary for 5JB1

• Entry DOI: 10.2210/pdb5jb1/pdb
• Related: 5J6R
• EMDB information: 8147
• Descriptor: Major capsid protein L1 (1 entity in total)
• Functional Keywords: capsid, t=7 icosahedral, virus-like particle, virus
• Biological source: Human papillomavirus type 59
• Total number of polymer chains: 6
• Total formula weight: 335870.51

Authors

Li, Z.H.,Yan, X.D.,Yu, H.,Zheng, Q.B.,Gu, Y.,Li, S.W. (deposition date: 2016-04-13, release date: 2016-05-18, Last modification date: 2024-05-29)

Primary citation

Li, Z.,Yan, X.,Yu, H.,Wang, D.,Song, S.,Li, Y.,He, M.,Hong, Q.,Zheng, Q.,Zhao, Q.,Gu, Y.,Zhang, J.,Janssen, M.E.,Cardone, G.,Olson, N.H.,Baker, T.S.,Li, S.,Xia, N.
The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction.
Structure, 24:874-885, 2016

PubMed Abstract: Cervical cancer is the second most prevalent malignant tumor among women worldwide. High-risk human papillomaviruses (HPVs) are believed to be the major causative pathogens of mucosal epithelial cancers including cervical cancer. The HPV capsid is made up of 360 copies of major (L1) and 72 copies of minor (L2) capsid proteins. To date, limited high-resolution structural information about the HPV capsid has hindered attempts to understand details concerning the mechanisms by which HPV assembles and infects cells. In this study, we have constructed a pseudo-atomic model of the HPV59 L1-only capsid and demonstrate that the C-terminal arm of L1 participates in virus-host interactions. Moreover, when conjugated to a scaffold protein, keyhole limpet hemocyanin (KLH), this arm is immunogenic in vivo. These results provide new insights that will help elucidate HPV biology, and hence pave a way for the design of next-generation HPV vaccines.

PubMed: 27276427
DOI: 10.1016/j.str.2016.04.008

Experimental method

ELECTRON MICROSCOPY (6 Å)