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Updated: Oct 10, 2026

An Ex Vivo Chicken Primary Bursal-cell Culture Model to Study Infectious Bursal Disease Virus Pathogenesis
07:26

An Ex Vivo Chicken Primary Bursal-cell Culture Model to Study Infectious Bursal Disease Virus Pathogenesis

Published on: October 4, 2018

VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane

E Lombardo1, A Maraver, I Espinosa

  • 1Department of Biología Molecular y Celular, Centro Nacional de Biotecnología, Cantoblanco, 28049 Madrid, Spain.

Virology
|November 18, 2000
PubMed

Insights

The Infectious bursal disease virus (IBDV) VP5 protein is crucial for virus spread and disease. VP5 accumulates in the plasma membrane, causing cell death and aiding IBDV progeny release.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Infectious bursal disease virus (IBDV) is a significant pathogen in poultry.
  • The nonstructural VP5 polypeptide is not essential for in vitro viral replication but impacts in vivo pathogenesis.
  • Understanding VP5's role is key to controlling IBDV spread and disease.

Purpose of the Study:

  • To characterize the expression and cellular localization of the IBDV VP5 protein.
  • To investigate the role of the exocytic pathway in VP5 transport.
  • To determine the cytotoxic effects of VP5 expression and its contribution to viral pathogenesis.

Main Methods:

  • Expression analysis of VP5 in chicken embryo fibroblasts, BSC-1 cells (recombinant vaccinia virus), and Cos-1 cells (transfection).
  • Immunofluorescence microscopy to visualize VP5 localization.
  • Brefeldin A treatment to assess the exocytic pathway's role.
  • Cytotoxicity assays to evaluate cell viability and morphology changes.

Main Results:

  • VP5 accumulates in the plasma membrane, consistent with predictions of a class II membrane protein.
  • VP5 transport to the plasma membrane requires an active exocytic pathway, as shown by Brefeldin A treatment.
  • VP5 expression is highly cytotoxic, leading to altered cell morphology, membrane disruption, and reduced cell viability.
  • Inhibition of VP5 transport to the membrane with Brefeldin A prevented cytotoxicity.

Conclusions:

  • VP5 is a plasma membrane-localized protein whose transport depends on the exocytic pathway.
  • VP5 expression induces significant cytotoxicity, suggesting a role in viral pathogenesis.
  • The findings indicate that VP5 is important for the release of IBDV progeny.

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