4EJR

Crystal structure of major capsid protein S domain from rabbit hemorrhagic disease virus

Summary for 4EJR

• Entry DOI: 10.2210/pdb4ejr/pdb
• Related: 4EGT 4J1P
• Descriptor: Major capsid protein VP60 (2 entities in total)
• Functional Keywords: viral protein, capsid protein
• Biological source: Rabbit hemorrhagic disease virus (RHDV)
• Total number of polymer chains: 2
• Total formula weight: 54416.57

Authors

Xu, F.,Ma, J.,Zhang, K.,Wang, X.,Sun, F. (deposition date: 2012-04-07, release date: 2013-01-30, Last modification date: 2023-09-13)

Primary citation

Wang, X.,Xu, F.,Liu, J.,Gao, B.,Liu, Y.,Zhai, Y.,Ma, J.,Zhang, K.,Baker, T.S.,Schulten, K.,Zheng, D.,Pang, H.,Sun, F.
Atomic model of rabbit hemorrhagic disease virus by cryo-electron microscopy and crystallography.
Plos Pathog., 9:e1003132-e1003132, 2013

PubMed Abstract: Rabbit hemorrhagic disease, first described in China in 1984, causes hemorrhagic necrosis of the liver. Its etiological agent, rabbit hemorrhagic disease virus (RHDV), belongs to the Lagovirus genus in the family Caliciviridae. The detailed molecular structure of any lagovirus capsid has yet to be determined. Here, we report a cryo-electron microscopic (cryoEM) reconstruction of wild-type RHDV at 6.5 Å resolution and the crystal structures of the shell (S) and protruding (P) domains of its major capsid protein, VP60, each at 2.0 Å resolution. From these data we built a complete atomic model of the RHDV capsid. VP60 has a conserved S domain and a specific P2 sub-domain that differs from those found in other caliciviruses. As seen in the shell portion of the RHDV cryoEM map, which was resolved to ~5.5 Å, the N-terminal arm domain of VP60 folds back onto its cognate S domain. Sequence alignments of VP60 from six groups of RHDV isolates revealed seven regions of high variation that could be mapped onto the surface of the P2 sub-domain and suggested three putative pockets might be responsible for binding to histo-blood group antigens. A flexible loop in one of these regions was shown to interact with rabbit tissue cells and contains an important epitope for anti-RHDV antibody production. Our study provides a reliable, pseudo-atomic model of a Lagovirus and suggests a new candidate for an efficient vaccine that can be used to protect rabbits from RHDV infection.

PubMed: 23341770
DOI: 10.1371/journal.ppat.1003132

Experimental method

X-RAY DIFFRACTION (2 Å)