Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The 2.6-Angstrom Structure of Infectious Bursal Disease Virus-Derived T=1 Particles Reveals New Stabilizing Elements of the Virus Capsid

29 Jun 2006

Abstract excerpt

Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is a double-stranded RNA virus that causes a highly contagious disease in young chickens leading to significant economic losses in the poultry industry. The VP2 protein, the only structural component of the IBDV icosahedral capsid, spontaneously assembles into T=1 subviral particles (SVP) when individually expressed as a chimeric gene....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Plant Virus Research Studies
Share to Virology and Viral Diseases
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16809295
DOI: 10.1128/jvi.00368-06

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The 2.6-Angstrom Structure of Infectious Bursal Disease Virus-Derived T=1 Particles Reveals New Stabilizing Elements of the Virus CapsidPMID 16809295Read ↗

Cryo-EM structures of infectious bursal disease viruses with different virulences provide insights into their assembly and invasionSemantic proximity Read ↗

C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid AssemblySemantic proximity Read ↗

Three-dimensional structure of infectious bursal disease virus determined by electron cryomicroscopySemantic proximity Read ↗

Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical roleSemantic proximity Read ↗

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

Infectious Bursal Disease Virus Hijacks Endosomal Membranes as the Scaffolding Structure for Viral ReplicationSemantic proximity Read ↗

A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stabilitySemantic proximity Read ↗

Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNASemantic proximity Read ↗

The Maturation Process of pVP2 Requires Assembly of Infectious Bursal Disease Virus CapsidsSemantic proximity Read ↗

Crystal Structure of an Aquabirnavirus Particle: Insights into Antigenic Diversity and Virulence DeterminismSemantic proximity Read ↗

Infectious Bursal Disease Virus-Host Interactions: Multifunctional Viral Proteins that Perform Multiple and Differing JobsSemantic proximity Read ↗

Molecular and Structural Bases for the Antigenicity of VP2 of Infectious Bursal Disease VirusSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.