Crystal structure of infectious bursal disease virus VP2 subviral particle at 2.6 Å resolution: Implications in virion assembly and immunogenicity

Lee, Cheng-Chung; Ko, Tzu‐Ping; Chou, Cheng‐Chun; Yoshimura, Masato; Doong, Shyue-Ru; Wang, Min-Ying; Wang, Andrew H.-J.

doi:10.1016/j.jsb.2006.02.014

Cited by 63 publications

(52 citation statements)

References 32 publications

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“…In addition, the IPNV VP2 trimer has a chlorine ion also located on the 3-old molecular axis between domains S and P, coordinated to the main chain amide of Ala199 of the three VP2 subunits. A chlorine ion at this location was also identified in IBDV VP2 (31). The presence of these ions may further stabilize the VP2 trimer, but their role could also be to seal the solvent channel present along the 3-fold axis (which is clearly seen in Fig.…”

Section: Resultsmentioning

confidence: 84%

“…The presence of a central metal stabilizing each trimer is thus also a conserved feature of the birnavirus particles. The cation is located on the 3-fold axis between domains B and S, occupying the Ca 2ϩ site observed in IBDV VP2 (23,31), coordinated by Asp26 (IPNV numbering) from the three subunits (Fig. 1B, inset).…”

Section: Resultsmentioning

confidence: 99%

“…The crystal structures of the SVPs of infectious bursal disease virus of poultry (IBDV) were reported by several groups (15,23,31) as well as the threedimensional (3D) structure of an intact Tϭ13l IBDV virion (15).…”

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confidence: 99%

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Crystal Structure of an Aquabirnavirus Particle: Insights into Antigenic Diversity and Virulence Determinism

Coulibaly

Chevalier

Delmas

et al. 2010

J Virol

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Infectious pancreatic necrosis virus (IPNV), a pathogen of salmon and trout, imposes a severe toll on the aquaculture and sea farming industries. IPNV belongs to the Aquabirnavirus genus in the Birnaviridae family of bisegmented double-stranded RNA viruses. The virions are nonenveloped with a T‫31؍‬l icosahedral capsid made by the coat protein VP2, the three-dimensional (3D) organization of which is known in detail for the family prototype, the infectious bursal disease virus (IBDV) of poultry. A salient feature of the birnavirus architecture is the presence of 260 trimeric spikes formed by VP2, projecting radially from the capsid. The spikes carry the principal antigenic sites as well as virulence and cell adaptation determinants. We report here the 3.4-Å resolution crystal structure of a subviral particle (SVP) of IPNV, containing 20 VP2 trimers organized with icosahedral symmetry. We show that, as expected, the SVPs have a very similar organization to the IBDV counterparts, with VP2 exhibiting the same overall 3D fold. However, the spikes are significantly different, displaying a more compact organization with tighter packing about the molecular 3-fold axis. Amino acids controlling virulence and cell culture adaptation cluster differently at the top of the spike, i.e., in a central bowl in IBDV and at the periphery in IPNV. In contrast, the spike base features an exposed groove, conserved across birnavirus genera, which contains an integrin-binding motif. Thus, in addition to revealing the viral antigenic determinants, the structure suggests that birnaviruses interact with different receptors for attachment and for cell internalization during entry.Birnaviruses form a distinct family of double-stranded RNA (dsRNA) viruses infecting vertebrates and invertebrates (18). Aquatic birnaviruses are the most abundant and diverse and are grouped in two separate genera: the Aquabirnavirus genus and the Blosnavirus genus, with infectious pancreatic necrosis virus (IPNV) and blotched snakehead virus (BSNV) (16) as respective type species. A third aquatic birnavirus of unassigned genus, Tellina virus 1, was recently described and found to be phylogenetically distant from the two established genera (40). However, the vast majority of aquatic birnaviruses are antigenically related to IPNV (i.e., belong to the Aquabirnavirus genus), regardless of host species or geographical origin (4,11,26,39). They are implicated as etiological agents of disease in a variety of mollusks and fish species important in aquaculture, causing pathologies such as infectious pancreatic necrosis in salmonids, nephroblastoma and branchionephritis in eels, and gill necrosis in clams (21,34,50). Viruses in the Aquabirnavirus genus display considerable antigenic diversity and have substantial differences in biological properties such as host range and optimal replication temperature. These features contrast with the properties of other birnaviruses, in particular those infecting terrestrial species (avibirnaviruses and entomobirnaviruses). Based on rec...

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Section: Resultsmentioning

confidence: 84%

Section: Resultsmentioning

confidence: 99%

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Crystal Structure of an Aquabirnavirus Particle: Insights into Antigenic Diversity and Virulence Determinism

Coulibaly

Chevalier

Delmas

et al. 2010

J Virol

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“…Our model for vaccine development is the IBDV VP2 capsid protein, which we tested as a platform to anchor foreign antigens. Based on the VP2 atomic structure resolved by X-ray crystallography (20)(21)(22), we evaluated its capacity to incorporate fused foreign peptides or proteins to specific sites, without interfering with its natural tendency to assemble into icosahedral capsids or helical tubes.…”

Section: Discussionmentioning

confidence: 99%

“…VP3 participates during capsid assembly as a canonical scaffolding protein (18,19). Expression of VP2 alone results in the assembly of ϳ23-nm-diameter Tϭ1 subviral particles (SVPs) (20)(21)(22). VP2 is folded into three domains, termed the projection (P), shell (S), and base (B) domains.…”

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confidence: 99%

Structural Basis for the Development of Avian Virus Capsids That Display Influenza Virus Proteins and Induce Protective Immunity

Pascual

Mata

Gómez-Blanco

et al. 2015

J Virol

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Bioengineering of viruses and virus-like particles (VLPs) is a well-established approach in the development of new and improved vaccines against viral and bacterial pathogens. We report here that the capsid of a major avian pathogen, infectious bursal disease virus (IBDV), can accommodate heterologous proteins to induce protective immunity. The structural units of the ϳ70-nmdiameter T‫31؍‬ IBDV capsid are trimers of VP2, which is made as a precursor (pVP2). The pVP2 C-terminal domain has an amphipathic ␣ helix that controls VP2 polymorphism. In the absence of the VP3 scaffolding protein, 466-residue pVP2 intermediates bearing this ␣ helix assemble into genuine VLPs only when expressed with an N-terminal His 6 tag (the HT-VP2-466 protein). HT-VP2-466 capsids are optimal for protein insertion, as they are large enough (cargo space, ϳ78,000 nm 3 ) and are assembled from a single protein. We explored HT-VP2-466-based chimeric capsids initially using enhanced green fluorescent protein (EGFP). The VLP assembly yield was efficient when we coexpressed EGFP-HT-VP2-466 and HT-VP2-466 from two recombinant baculoviruses. The native EGFP structure (ϳ240 copies/virion) was successfully inserted in a functional form, as VLPs were fluorescent, and three-dimensional cryo-electron microscopy showed that the EGFP molecules incorporated at the inner capsid surface. Immunization of mice with purified EGFP-VLPs elicited anti-EGFP antibodies. We also inserted hemagglutinin (HA) and matrix (M2) protein epitopes derived from the mouse-adapted A/PR/8/34 influenza virus and engineered several HA-and M2-derived chimeric capsids. Mice immunized with VLPs containing the HA stalk, an M2 fragment, or both antigens developed full protection against viral challenge. IMPORTANCEVirus-like particles (VLPs) are multimeric protein cages that mimic the infectious virus capsid and are potential candidates as nonliving vaccines that induce long-lasting protection. Chimeric VLPs can display or include foreign antigens, which could be a conserved epitope to elicit broadly neutralizing antibodies or several variable epitopes effective against a large number of viral strains. We report the biochemical, structural, and immunological characterization of chimeric VLPs derived from infectious bursal disease virus (IBDV), an important poultry pathogen. To test the potential of IBDV VLPs as a vaccine vehicle, we used the enhanced green fluorescent protein and two fragments derived from the hemagglutinin and the M2 matrix protein of the human murine-adapted influenza virus. The IBDV capsid protein fused to influenza virus peptides formed assemblies able to protect mice against viral challenge. Our studies establish the basis for a new generation of multivalent IBDV-based vaccines.

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Infectious Bursal Disease

Eterradossi¹,

Saif²

2019

Diseases of Poultry

130

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Crystal structure of infectious bursal disease virus VP2 subviral particle at 2.6 Å resolution: Implications in virion assembly and immunogenicity

Cited by 63 publications

References 32 publications

Crystal Structure of an Aquabirnavirus Particle: Insights into Antigenic Diversity and Virulence Determinism

Crystal Structure of an Aquabirnavirus Particle: Insights into Antigenic Diversity and Virulence Determinism

Structural Basis for the Development of Avian Virus Capsids That Display Influenza Virus Proteins and Induce Protective Immunity

Infectious Bursal Disease

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