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Related Concept Videos

Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

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Related Experiment Video

Updated: Jun 20, 2026

Expression and Purification of Virus-like Particles for Vaccination
06:17

Expression and Purification of Virus-like Particles for Vaccination

Published on: June 2, 2016

Prokaryotically expressed IBDV VP2 virus-like particles: Stability and protective efficacy.

Jinjin Zhang1, Xuegang Zhang1, Lihua Li2

  • 1State Key Laboratory of Animal Disease Control and Prevention, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, PR China.

Microbial Pathogenesis
|June 18, 2026
PubMed
Summary

New virus-like particles (VLPs) offer a stable and effective vaccine candidate against Infectious Bursal Disease Virus (IBDV) in chickens, showing high immunogenicity and safety without immunosuppression risks.

Keywords:
Infectious bursal disease virusMolecular dynamics simulationsStabilityVaccineVirus-like particles

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Last Updated: Jun 20, 2026

Expression and Purification of Virus-like Particles for Vaccination
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Vaccinia Reporter Viruses for Quantifying Viral Function at All Stages of Gene Expression
10:48

Vaccinia Reporter Viruses for Quantifying Viral Function at All Stages of Gene Expression

Published on: May 15, 2014

Area of Science:

  • Veterinary Virology
  • Vaccine Development
  • Structural Biology

Background:

  • Infectious Bursal Disease Virus (IBDV) causes significant immunosuppression in chickens.
  • Traditional IBDV vaccines pose potential safety concerns.
  • Virus-like particles (VLPs) present a promising alternative due to high immunogenicity and safety, but their stability mechanisms require elucidation.

Purpose of the Study:

  • To investigate the structural basis for the stability of IBDV virus-like particles (VLPs).
  • To evaluate the efficacy of IBDV VLPs as a vaccine candidate.
  • To provide insights for designing more stable VLP vaccines.

Main Methods:

  • Expression of IBDV VP2 protein in Escherichia coli and self-assembly into VLPs.
  • Stability assays at 4°C and 37°C.
  • Circular dichroism (CD) and molecular dynamics (MD) simulations for structural analysis.
  • Animal vaccination experiments to assess immunogenicity and protection.

Main Results:

  • IBDV VLPs demonstrated enhanced stability compared to monomeric VP2, remaining intact for over 180 days at 4°C.
  • Structural analyses revealed VLPs possess higher α-helix content, lower solvent-accessible surface area, and a more compact conformation.
  • VLPs exhibited reduced flexibility at 37°C due to inter-subunit conformational locking, a short-term anti-Arrhenius behavior.
  • Vaccination with IBDV VLPs induced dose-dependent high antibody titers and conferred complete protection against IBDV challenge without bursal lesions.

Conclusions:

  • The structural characteristics of IBDV VLPs contribute to their superior stability.
  • IBDV VLPs represent a stable and effective vaccine candidate, offering complete protection.
  • This study provides valuable insights into the structure-stability relationship of VLPs for future vaccine design.