ArticlePLoS pathogens2013
Atomic model of rabbit hemorrhagic disease virus by cryo-electron microscopy and crystallography.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 113 citations in OpenAlex.
- Molecular characterization of rabbit hemorrhagic disease virus type 2 and long-lasting protection conferred by a VLP-based vaccine.BMC veterinary research · 2026Article
- Mutational analysis of human norovirus VP2 elucidates critical molecular interactions for virus assembly.Journal of virology · 2026Article
- Detection and Characterisation of The 'A' Variant of Rabbit Haemorrhagic Disease (RHDVa, GI.1a) Over a Decade (2013-2023) in Italy.Transboundary and emerging diseases · 2026Article
- Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.PLoS pathogens · 2025Article
- Atomistic simulations of intact virus capsids: A computational challenge worth the scientific payoff.Current opinion in structural biology · 2025Review
- Precocious Eimeria magna transgenically expressing RHDV P2 subdomain induces immune responses in rabbits.NPJ vaccines · 2025Article
- Epitope mapping of a neutralizing antibody against rabbit hemorrhagic disease virus GI.2.Veterinary research · 2025Article
- Near-atomic structures of RHDV reveal insights into capsid assembly and different conformations between mature virion and VLP.Journal of virology · 2024Article
- Characterisation ofInternational journal of molecular sciences · 2024Review
- Serological characterisation ofJournal of veterinary research · 2024Article
- Recombination between non-structural and structural genes as a mechanism of selection in lagoviruses: The evolutionary dead-end of an RHDV2 isolated from European hare.Virus research · 2024Article
- A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity.Nature communications · 2023Article
- Article
- Characterization of surface-exposed structural loops as insertion sites for foreign antigen delivery in calicivirus-derived VLP platform.Frontiers in microbiology · 2023Article
- Co-circulation of GI.1 and GI.2 genotypes of rabbit hemorrhagic disease virus in Egypt.Virusdisease · 2022Article
- Structural Basis for Rabbit Hemorrhagic Disease Virus Antibody Specificity.Journal of virology · 2022Article
- Atomic Structure of the Human Sapovirus Capsid Reveals a Unique Capsid Protein Conformation in Caliciviruses.Journal of virology · 2022Article
- Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity.Nature communications · 2022Article
- Article
- Immunogenicity of Multi-Target Chimeric RHDV Virus-Like Particles Delivering Foreign B-Cell Epitopes.Vaccines · 2022Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 8 institutions in 2 countries.
Funding
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.
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